data_7Q0C
# 
_entry.id   7Q0C 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.384 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7Q0C         pdb_00007q0c 10.2210/pdb7q0c/pdb 
WWPDB D_1292118532 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2022-01-12 
2 'Structure model' 1 1 2022-01-26 
3 'Structure model' 1 2 2024-01-31 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation                      
2 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
3 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7Q0C 
_pdbx_database_status.recvd_initial_deposition_date   2021-10-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              grazulis@ibt.lt 
_pdbx_contact_author.name_first         Saulius 
_pdbx_contact_author.name_last          Grazulis 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7928-5218 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Paketuryte-Latve, V.' 1 0000-0003-0919-7826 
'Smirnov, A.'          2 0000-0001-5080-9367 
'Manakova, E.'         3 0000-0002-6027-2265 
'Grazulis, S.'         4 0000-0002-7928-5218 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Int J Mol Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1422-0067 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            23 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Methyl 2-Halo-4-Substituted-5-Sulfamoyl-Benzoates as High Affinity and Selective Inhibitors of Carbonic Anhydrase IX.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/ijms23010130 
_citation.pdbx_database_id_PubMed   35008553 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'       1  ? 
primary 'Capkauskaite, E.'     2  ? 
primary 'Paketuryte-Latve, V.' 3  ? 
primary 'Smirnov, A.'          4  ? 
primary 'Leitans, J.'          5  ? 
primary 'Kazaks, A.'           6  ? 
primary 'Dvinskis, E.'         7  ? 
primary 'Stancaitis, L.'       8  ? 
primary 'Mickeviciute, A.'     9  ? 
primary 'Jachno, J.'           10 ? 
primary 'Jezepcikas, L.'       11 ? 
primary 'Linkuviene, V.'       12 ? 
primary 'Sakalauskas, A.'      13 ? 
primary 'Manakova, E.'         14 ? 
primary 'Grazulis, S.'         15 ? 
primary 'Matuliene, J.'        16 ? 
primary 'Tars, K.'             17 ? 
primary 'Matulis, D.'          18 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                         29242.992 2   4.2.1.1 
'A65S, N67Q, I91L, F130V, V134L, L203A.' ? ? 
2 non-polymer syn 'ZINC ION'                                                     65.409    2   ?       ? ? ? 
3 non-polymer syn 'methyl 2-chloranyl-4-cyclohexylsulfanyl-5-sulfamoyl-benzoate' 363.880   2   ?       ? ? ? 
4 non-polymer syn 'ACETATE ION'                                                  59.044    1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                           78.133    2   ?       ? ? ? 
6 water       nat water                                                          18.015    602 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFQVEFDDSQDKAVLK
GGPLDGTYRLLQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDVGKALQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLAECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFQVEFDDSQDKAVLK
GGPLDGTYRLLQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDVGKALQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLAECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                     ZN  
3 'methyl 2-chloranyl-4-cyclohexylsulfanyl-5-sulfamoyl-benzoate' 7VZ 
4 'ACETATE ION'                                                  ACT 
5 'DIMETHYL SULFOXIDE'                                           DMS 
6 water                                                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  SER n 
1 66  PHE n 
1 67  GLN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  LEU n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 VAL n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 LEU n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 ALA n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'L21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
7VZ non-polymer         . 'methyl 2-chloranyl-4-cyclohexylsulfanyl-5-sulfamoyl-benzoate' ? 'C14 H18 Cl N O4 S2' 363.880 
ACT non-polymer         . 'ACETATE ION'                                                  ? 'C2 H3 O2 -1'        59.044  
ALA 'L-peptide linking' y ALANINE                                                        ? 'C3 H7 N O2'         89.093  
ARG 'L-peptide linking' y ARGININE                                                       ? 'C6 H15 N4 O2 1'     175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                     ? 'C4 H8 N2 O3'        132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                ? 'C4 H7 N O4'         133.103 
CYS 'L-peptide linking' y CYSTEINE                                                       ? 'C3 H7 N O2 S'       121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                           ? 'C2 H6 O S'          78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                      ? 'C5 H10 N2 O3'       146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                ? 'C5 H9 N O4'         147.129 
GLY 'peptide linking'   y GLYCINE                                                        ? 'C2 H5 N O2'         75.067  
HIS 'L-peptide linking' y HISTIDINE                                                      ? 'C6 H10 N3 O2 1'     156.162 
HOH non-polymer         . WATER                                                          ? 'H2 O'               18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                     ? 'C6 H13 N O2'        131.173 
LEU 'L-peptide linking' y LEUCINE                                                        ? 'C6 H13 N O2'        131.173 
LYS 'L-peptide linking' y LYSINE                                                         ? 'C6 H15 N2 O2 1'     147.195 
MET 'L-peptide linking' y METHIONINE                                                     ? 'C5 H11 N O2 S'      149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                  ? 'C9 H11 N O2'        165.189 
PRO 'L-peptide linking' y PROLINE                                                        ? 'C5 H9 N O2'         115.130 
SER 'L-peptide linking' y SERINE                                                         ? 'C3 H7 N O3'         105.093 
THR 'L-peptide linking' y THREONINE                                                      ? 'C4 H9 N O3'         119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                     ? 'C11 H12 N2 O2'      204.225 
TYR 'L-peptide linking' y TYROSINE                                                       ? 'C9 H11 N O3'        181.189 
VAL 'L-peptide linking' y VALINE                                                         ? 'C5 H11 N O2'        117.146 
ZN  non-polymer         . 'ZINC ION'                                                     ? 'Zn 2'               65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 CYS 205 205 205 CYS CYS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   HIS 3   3   ?   ?   ?   B . n 
B 1 4   HIS 4   4   4   HIS HIS B . n 
B 1 5   TRP 5   5   5   TRP TRP B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   TYR 7   7   7   TYR TYR B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  HIS 10  10  10  HIS HIS B . n 
B 1 11  ASN 11  11  11  ASN ASN B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  HIS 15  15  15  HIS HIS B . n 
B 1 16  TRP 16  16  16  TRP TRP B . n 
B 1 17  HIS 17  17  17  HIS HIS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  HIS 36  36  36  HIS HIS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  GLN 53  53  53  GLN GLN B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  ASN 62  62  62  ASN ASN B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  GLN 67  67  67  GLN GLN B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  PRO 83  83  83  PRO PRO B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  LEU 91  91  91  LEU LEU B . n 
B 1 92  GLN 92  92  92  GLN GLN B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  TRP 97  97  97  TRP TRP B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 GLN 103 103 103 GLN GLN B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 HIS 122 122 122 HIS HIS B . n 
B 1 123 TRP 123 123 123 TRP TRP B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 THR 125 125 125 THR THR B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 TYR 127 127 127 TYR TYR B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 VAL 130 130 130 VAL VAL B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 ALA 133 133 133 ALA ALA B . n 
B 1 134 LEU 134 134 134 LEU LEU B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLN 136 136 136 GLN GLN B . n 
B 1 137 PRO 137 137 137 PRO PRO B . n 
B 1 138 ASP 138 138 138 ASP ASP B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ALA 141 141 141 ALA ALA B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 ILE 145 145 145 ILE ILE B . n 
B 1 146 PHE 146 146 146 PHE PHE B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 VAL 149 149 149 VAL VAL B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 SER 151 151 151 SER SER B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 PRO 154 154 154 PRO PRO B . n 
B 1 155 GLY 155 155 155 GLY GLY B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 GLN 157 157 157 GLN GLN B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 VAL 160 160 160 VAL VAL B . n 
B 1 161 ASP 161 161 161 ASP ASP B . n 
B 1 162 VAL 162 162 162 VAL VAL B . n 
B 1 163 LEU 163 163 163 LEU LEU B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 SER 165 165 165 SER SER B . n 
B 1 166 ILE 166 166 166 ILE ILE B . n 
B 1 167 LYS 167 167 167 LYS LYS B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 LYS 169 169 169 LYS LYS B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 LYS 171 171 171 LYS LYS B . n 
B 1 172 SER 172 172 172 SER SER B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 ASP 174 174 174 ASP ASP B . n 
B 1 175 PHE 175 175 175 PHE PHE B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 ASN 177 177 177 ASN ASN B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 PRO 180 180 180 PRO PRO B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 SER 187 187 187 SER SER B . n 
B 1 188 LEU 188 188 188 LEU LEU B . n 
B 1 189 ASP 189 189 189 ASP ASP B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TRP 191 191 191 TRP TRP B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 PRO 194 194 194 PRO PRO B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 LEU 202 202 202 LEU LEU B . n 
B 1 203 ALA 203 203 203 ALA ALA B . n 
B 1 204 GLU 204 204 204 GLU GLU B . n 
B 1 205 CYS 205 205 205 CYS CYS B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 THR 207 207 207 THR THR B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 ILE 209 209 209 ILE ILE B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 GLU 213 213 213 GLU GLU B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 ILE 215 215 215 ILE ILE B . n 
B 1 216 SER 216 216 216 SER SER B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 VAL 222 222 222 VAL VAL B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 PHE 225 225 225 PHE PHE B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 LYS 227 227 227 LYS LYS B . n 
B 1 228 LEU 228 228 228 LEU LEU B . n 
B 1 229 ASN 229 229 229 ASN ASN B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 GLY 232 232 232 GLY GLY B . n 
B 1 233 GLU 233 233 233 GLU GLU B . n 
B 1 234 GLY 234 234 234 GLY GLY B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 PRO 236 236 236 PRO PRO B . n 
B 1 237 GLU 237 237 237 GLU GLU B . n 
B 1 238 GLU 238 238 238 GLU GLU B . n 
B 1 239 LEU 239 239 239 LEU LEU B . n 
B 1 240 MET 240 240 240 MET MET B . n 
B 1 241 VAL 241 241 241 VAL VAL B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 ASN 243 243 243 ASN ASN B . n 
B 1 244 TRP 244 244 244 TRP TRP B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 PRO 246 246 246 PRO PRO B . n 
B 1 247 ALA 247 247 247 ALA ALA B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 ARG 253 253 253 ARG ARG B . n 
B 1 254 GLN 254 254 254 GLN GLN B . n 
B 1 255 ILE 255 255 255 ILE ILE B . n 
B 1 256 LYS 256 256 256 LYS LYS B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 SER 258 258 258 SER SER B . n 
B 1 259 PHE 259 259 259 PHE PHE B . n 
B 1 260 LYS 260 260 260 LYS LYS B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1   301 1   ZN  ZN  A . 
D 3 7VZ 1   302 2   7VZ EA3 A . 
E 4 ACT 1   303 4   ACT ACT A . 
F 5 DMS 1   304 1   DMS DMS A . 
G 2 ZN  1   301 2   ZN  ZN  B . 
H 3 7VZ 1   302 1   7VZ EA3 B . 
I 5 DMS 1   303 2   DMS DMS B . 
J 6 HOH 1   401 308 HOH HOH A . 
J 6 HOH 2   402 270 HOH HOH A . 
J 6 HOH 3   403 580 HOH HOH A . 
J 6 HOH 4   404 556 HOH HOH A . 
J 6 HOH 5   405 577 HOH HOH A . 
J 6 HOH 6   406 383 HOH HOH A . 
J 6 HOH 7   407 101 HOH HOH A . 
J 6 HOH 8   408 462 HOH HOH A . 
J 6 HOH 9   409 328 HOH HOH A . 
J 6 HOH 10  410 392 HOH HOH A . 
J 6 HOH 11  411 297 HOH HOH A . 
J 6 HOH 12  412 583 HOH HOH A . 
J 6 HOH 13  413 214 HOH HOH A . 
J 6 HOH 14  414 255 HOH HOH A . 
J 6 HOH 15  415 292 HOH HOH A . 
J 6 HOH 16  416 380 HOH HOH A . 
J 6 HOH 17  417 458 HOH HOH A . 
J 6 HOH 18  418 385 HOH HOH A . 
J 6 HOH 19  419 136 HOH HOH A . 
J 6 HOH 20  420 403 HOH HOH A . 
J 6 HOH 21  421 253 HOH HOH A . 
J 6 HOH 22  422 390 HOH HOH A . 
J 6 HOH 23  423 431 HOH HOH A . 
J 6 HOH 24  424 335 HOH HOH A . 
J 6 HOH 25  425 440 HOH HOH A . 
J 6 HOH 26  426 358 HOH HOH A . 
J 6 HOH 27  427 191 HOH HOH A . 
J 6 HOH 28  428 460 HOH HOH A . 
J 6 HOH 29  429 427 HOH HOH A . 
J 6 HOH 30  430 412 HOH HOH A . 
J 6 HOH 31  431 180 HOH HOH A . 
J 6 HOH 32  432 450 HOH HOH A . 
J 6 HOH 33  433 104 HOH HOH A . 
J 6 HOH 34  434 219 HOH HOH A . 
J 6 HOH 35  435 216 HOH HOH A . 
J 6 HOH 36  436 547 HOH HOH A . 
J 6 HOH 37  437 500 HOH HOH A . 
J 6 HOH 38  438 74  HOH HOH A . 
J 6 HOH 39  439 22  HOH HOH A . 
J 6 HOH 40  440 118 HOH HOH A . 
J 6 HOH 41  441 138 HOH HOH A . 
J 6 HOH 42  442 264 HOH HOH A . 
J 6 HOH 43  443 333 HOH HOH A . 
J 6 HOH 44  444 64  HOH HOH A . 
J 6 HOH 45  445 539 HOH HOH A . 
J 6 HOH 46  446 77  HOH HOH A . 
J 6 HOH 47  447 160 HOH HOH A . 
J 6 HOH 48  448 119 HOH HOH A . 
J 6 HOH 49  449 163 HOH HOH A . 
J 6 HOH 50  450 529 HOH HOH A . 
J 6 HOH 51  451 289 HOH HOH A . 
J 6 HOH 52  452 25  HOH HOH A . 
J 6 HOH 53  453 121 HOH HOH A . 
J 6 HOH 54  454 91  HOH HOH A . 
J 6 HOH 55  455 35  HOH HOH A . 
J 6 HOH 56  456 284 HOH HOH A . 
J 6 HOH 57  457 226 HOH HOH A . 
J 6 HOH 58  458 63  HOH HOH A . 
J 6 HOH 59  459 508 HOH HOH A . 
J 6 HOH 60  460 388 HOH HOH A . 
J 6 HOH 61  461 41  HOH HOH A . 
J 6 HOH 62  462 92  HOH HOH A . 
J 6 HOH 63  463 361 HOH HOH A . 
J 6 HOH 64  464 13  HOH HOH A . 
J 6 HOH 65  465 52  HOH HOH A . 
J 6 HOH 66  466 381 HOH HOH A . 
J 6 HOH 67  467 5   HOH HOH A . 
J 6 HOH 68  468 1   HOH HOH A . 
J 6 HOH 69  469 11  HOH HOH A . 
J 6 HOH 70  470 227 HOH HOH A . 
J 6 HOH 71  471 38  HOH HOH A . 
J 6 HOH 72  472 16  HOH HOH A . 
J 6 HOH 73  473 46  HOH HOH A . 
J 6 HOH 74  474 2   HOH HOH A . 
J 6 HOH 75  475 128 HOH HOH A . 
J 6 HOH 76  476 299 HOH HOH A . 
J 6 HOH 77  477 145 HOH HOH A . 
J 6 HOH 78  478 254 HOH HOH A . 
J 6 HOH 79  479 153 HOH HOH A . 
J 6 HOH 80  480 59  HOH HOH A . 
J 6 HOH 81  481 236 HOH HOH A . 
J 6 HOH 82  482 10  HOH HOH A . 
J 6 HOH 83  483 276 HOH HOH A . 
J 6 HOH 84  484 193 HOH HOH A . 
J 6 HOH 85  485 379 HOH HOH A . 
J 6 HOH 86  486 7   HOH HOH A . 
J 6 HOH 87  487 362 HOH HOH A . 
J 6 HOH 88  488 296 HOH HOH A . 
J 6 HOH 89  489 137 HOH HOH A . 
J 6 HOH 90  490 234 HOH HOH A . 
J 6 HOH 91  491 203 HOH HOH A . 
J 6 HOH 92  492 133 HOH HOH A . 
J 6 HOH 93  493 312 HOH HOH A . 
J 6 HOH 94  494 60  HOH HOH A . 
J 6 HOH 95  495 288 HOH HOH A . 
J 6 HOH 96  496 377 HOH HOH A . 
J 6 HOH 97  497 432 HOH HOH A . 
J 6 HOH 98  498 189 HOH HOH A . 
J 6 HOH 99  499 424 HOH HOH A . 
J 6 HOH 100 500 19  HOH HOH A . 
J 6 HOH 101 501 83  HOH HOH A . 
J 6 HOH 102 502 230 HOH HOH A . 
J 6 HOH 103 503 72  HOH HOH A . 
J 6 HOH 104 504 184 HOH HOH A . 
J 6 HOH 105 505 444 HOH HOH A . 
J 6 HOH 106 506 345 HOH HOH A . 
J 6 HOH 107 507 66  HOH HOH A . 
J 6 HOH 108 508 231 HOH HOH A . 
J 6 HOH 109 509 235 HOH HOH A . 
J 6 HOH 110 510 186 HOH HOH A . 
J 6 HOH 111 511 183 HOH HOH A . 
J 6 HOH 112 512 122 HOH HOH A . 
J 6 HOH 113 513 300 HOH HOH A . 
J 6 HOH 114 514 447 HOH HOH A . 
J 6 HOH 115 515 330 HOH HOH A . 
J 6 HOH 116 516 263 HOH HOH A . 
J 6 HOH 117 517 472 HOH HOH A . 
J 6 HOH 118 518 124 HOH HOH A . 
J 6 HOH 119 519 29  HOH HOH A . 
J 6 HOH 120 520 382 HOH HOH A . 
J 6 HOH 121 521 98  HOH HOH A . 
J 6 HOH 122 522 279 HOH HOH A . 
J 6 HOH 123 523 139 HOH HOH A . 
J 6 HOH 124 524 200 HOH HOH A . 
J 6 HOH 125 525 387 HOH HOH A . 
J 6 HOH 126 526 3   HOH HOH A . 
J 6 HOH 127 527 433 HOH HOH A . 
J 6 HOH 128 528 48  HOH HOH A . 
J 6 HOH 129 529 327 HOH HOH A . 
J 6 HOH 130 530 33  HOH HOH A . 
J 6 HOH 131 531 486 HOH HOH A . 
J 6 HOH 132 532 245 HOH HOH A . 
J 6 HOH 133 533 155 HOH HOH A . 
J 6 HOH 134 534 115 HOH HOH A . 
J 6 HOH 135 535 291 HOH HOH A . 
J 6 HOH 136 536 206 HOH HOH A . 
J 6 HOH 137 537 220 HOH HOH A . 
J 6 HOH 138 538 50  HOH HOH A . 
J 6 HOH 139 539 51  HOH HOH A . 
J 6 HOH 140 540 384 HOH HOH A . 
J 6 HOH 141 541 131 HOH HOH A . 
J 6 HOH 142 542 88  HOH HOH A . 
J 6 HOH 143 543 42  HOH HOH A . 
J 6 HOH 144 544 452 HOH HOH A . 
J 6 HOH 145 545 570 HOH HOH A . 
J 6 HOH 146 546 171 HOH HOH A . 
J 6 HOH 147 547 67  HOH HOH A . 
J 6 HOH 148 548 196 HOH HOH A . 
J 6 HOH 149 549 271 HOH HOH A . 
J 6 HOH 150 550 532 HOH HOH A . 
J 6 HOH 151 551 237 HOH HOH A . 
J 6 HOH 152 552 82  HOH HOH A . 
J 6 HOH 153 553 156 HOH HOH A . 
J 6 HOH 154 554 378 HOH HOH A . 
J 6 HOH 155 555 197 HOH HOH A . 
J 6 HOH 156 556 99  HOH HOH A . 
J 6 HOH 157 557 44  HOH HOH A . 
J 6 HOH 158 558 68  HOH HOH A . 
J 6 HOH 159 559 242 HOH HOH A . 
J 6 HOH 160 560 342 HOH HOH A . 
J 6 HOH 161 561 36  HOH HOH A . 
J 6 HOH 162 562 40  HOH HOH A . 
J 6 HOH 163 563 37  HOH HOH A . 
J 6 HOH 164 564 316 HOH HOH A . 
J 6 HOH 165 565 134 HOH HOH A . 
J 6 HOH 166 566 310 HOH HOH A . 
J 6 HOH 167 567 114 HOH HOH A . 
J 6 HOH 168 568 45  HOH HOH A . 
J 6 HOH 169 569 322 HOH HOH A . 
J 6 HOH 170 570 218 HOH HOH A . 
J 6 HOH 171 571 568 HOH HOH A . 
J 6 HOH 172 572 164 HOH HOH A . 
J 6 HOH 173 573 359 HOH HOH A . 
J 6 HOH 174 574 314 HOH HOH A . 
J 6 HOH 175 575 393 HOH HOH A . 
J 6 HOH 176 576 443 HOH HOH A . 
J 6 HOH 177 577 589 HOH HOH A . 
J 6 HOH 178 578 334 HOH HOH A . 
J 6 HOH 179 579 6   HOH HOH A . 
J 6 HOH 180 580 301 HOH HOH A . 
J 6 HOH 181 581 389 HOH HOH A . 
J 6 HOH 182 582 165 HOH HOH A . 
J 6 HOH 183 583 391 HOH HOH A . 
J 6 HOH 184 584 602 HOH HOH A . 
J 6 HOH 185 585 108 HOH HOH A . 
J 6 HOH 186 586 355 HOH HOH A . 
J 6 HOH 187 587 414 HOH HOH A . 
J 6 HOH 188 588 190 HOH HOH A . 
J 6 HOH 189 589 332 HOH HOH A . 
J 6 HOH 190 590 81  HOH HOH A . 
J 6 HOH 191 591 435 HOH HOH A . 
J 6 HOH 192 592 117 HOH HOH A . 
J 6 HOH 193 593 509 HOH HOH A . 
J 6 HOH 194 594 201 HOH HOH A . 
J 6 HOH 195 595 347 HOH HOH A . 
J 6 HOH 196 596 320 HOH HOH A . 
J 6 HOH 197 597 140 HOH HOH A . 
J 6 HOH 198 598 277 HOH HOH A . 
J 6 HOH 199 599 57  HOH HOH A . 
J 6 HOH 200 600 173 HOH HOH A . 
J 6 HOH 201 601 28  HOH HOH A . 
J 6 HOH 202 602 54  HOH HOH A . 
J 6 HOH 203 603 209 HOH HOH A . 
J 6 HOH 204 604 449 HOH HOH A . 
J 6 HOH 205 605 574 HOH HOH A . 
J 6 HOH 206 606 313 HOH HOH A . 
J 6 HOH 207 607 488 HOH HOH A . 
J 6 HOH 208 608 174 HOH HOH A . 
J 6 HOH 209 609 581 HOH HOH A . 
J 6 HOH 210 610 204 HOH HOH A . 
J 6 HOH 211 611 213 HOH HOH A . 
J 6 HOH 212 612 287 HOH HOH A . 
J 6 HOH 213 613 275 HOH HOH A . 
J 6 HOH 214 614 243 HOH HOH A . 
J 6 HOH 215 615 487 HOH HOH A . 
J 6 HOH 216 616 386 HOH HOH A . 
J 6 HOH 217 617 109 HOH HOH A . 
J 6 HOH 218 618 311 HOH HOH A . 
J 6 HOH 219 619 413 HOH HOH A . 
J 6 HOH 220 620 106 HOH HOH A . 
J 6 HOH 221 621 290 HOH HOH A . 
J 6 HOH 222 622 304 HOH HOH A . 
J 6 HOH 223 623 410 HOH HOH A . 
J 6 HOH 224 624 375 HOH HOH A . 
J 6 HOH 225 625 129 HOH HOH A . 
J 6 HOH 226 626 445 HOH HOH A . 
J 6 HOH 227 627 526 HOH HOH A . 
J 6 HOH 228 628 367 HOH HOH A . 
J 6 HOH 229 629 267 HOH HOH A . 
J 6 HOH 230 630 394 HOH HOH A . 
J 6 HOH 231 631 194 HOH HOH A . 
J 6 HOH 232 632 429 HOH HOH A . 
J 6 HOH 233 633 318 HOH HOH A . 
J 6 HOH 234 634 599 HOH HOH A . 
J 6 HOH 235 635 210 HOH HOH A . 
J 6 HOH 236 636 298 HOH HOH A . 
J 6 HOH 237 637 238 HOH HOH A . 
J 6 HOH 238 638 30  HOH HOH A . 
J 6 HOH 239 639 233 HOH HOH A . 
J 6 HOH 240 640 451 HOH HOH A . 
J 6 HOH 241 641 354 HOH HOH A . 
J 6 HOH 242 642 69  HOH HOH A . 
J 6 HOH 243 643 461 HOH HOH A . 
J 6 HOH 244 644 422 HOH HOH A . 
J 6 HOH 245 645 540 HOH HOH A . 
J 6 HOH 246 646 215 HOH HOH A . 
J 6 HOH 247 647 524 HOH HOH A . 
J 6 HOH 248 648 593 HOH HOH A . 
J 6 HOH 249 649 563 HOH HOH A . 
J 6 HOH 250 650 374 HOH HOH A . 
J 6 HOH 251 651 495 HOH HOH A . 
J 6 HOH 252 652 262 HOH HOH A . 
J 6 HOH 253 653 491 HOH HOH A . 
J 6 HOH 254 654 116 HOH HOH A . 
J 6 HOH 255 655 405 HOH HOH A . 
J 6 HOH 256 656 248 HOH HOH A . 
J 6 HOH 257 657 150 HOH HOH A . 
J 6 HOH 258 658 364 HOH HOH A . 
J 6 HOH 259 659 350 HOH HOH A . 
J 6 HOH 260 660 282 HOH HOH A . 
J 6 HOH 261 661 148 HOH HOH A . 
J 6 HOH 262 662 441 HOH HOH A . 
J 6 HOH 263 663 533 HOH HOH A . 
J 6 HOH 264 664 395 HOH HOH A . 
J 6 HOH 265 665 61  HOH HOH A . 
J 6 HOH 266 666 519 HOH HOH A . 
J 6 HOH 267 667 521 HOH HOH A . 
J 6 HOH 268 668 471 HOH HOH A . 
J 6 HOH 269 669 325 HOH HOH A . 
J 6 HOH 270 670 601 HOH HOH A . 
J 6 HOH 271 671 463 HOH HOH A . 
J 6 HOH 272 672 505 HOH HOH A . 
J 6 HOH 273 673 97  HOH HOH A . 
J 6 HOH 274 674 457 HOH HOH A . 
J 6 HOH 275 675 401 HOH HOH A . 
J 6 HOH 276 676 373 HOH HOH A . 
J 6 HOH 277 677 496 HOH HOH A . 
J 6 HOH 278 678 419 HOH HOH A . 
J 6 HOH 279 679 564 HOH HOH A . 
J 6 HOH 280 680 212 HOH HOH A . 
J 6 HOH 281 681 251 HOH HOH A . 
J 6 HOH 282 682 315 HOH HOH A . 
J 6 HOH 283 683 421 HOH HOH A . 
J 6 HOH 284 684 494 HOH HOH A . 
J 6 HOH 285 685 259 HOH HOH A . 
J 6 HOH 286 686 541 HOH HOH A . 
J 6 HOH 287 687 464 HOH HOH A . 
J 6 HOH 288 688 368 HOH HOH A . 
J 6 HOH 289 689 569 HOH HOH A . 
J 6 HOH 290 690 376 HOH HOH A . 
J 6 HOH 291 691 512 HOH HOH A . 
J 6 HOH 292 692 517 HOH HOH A . 
J 6 HOH 293 693 439 HOH HOH A . 
J 6 HOH 294 694 446 HOH HOH A . 
J 6 HOH 295 695 365 HOH HOH A . 
J 6 HOH 296 696 307 HOH HOH A . 
J 6 HOH 297 697 319 HOH HOH A . 
J 6 HOH 298 698 466 HOH HOH A . 
J 6 HOH 299 699 448 HOH HOH A . 
J 6 HOH 300 700 600 HOH HOH A . 
J 6 HOH 301 701 468 HOH HOH A . 
J 6 HOH 302 702 467 HOH HOH A . 
J 6 HOH 303 703 317 HOH HOH A . 
K 6 HOH 1   401 470 HOH HOH B . 
K 6 HOH 2   402 240 HOH HOH B . 
K 6 HOH 3   403 587 HOH HOH B . 
K 6 HOH 4   404 595 HOH HOH B . 
K 6 HOH 5   405 459 HOH HOH B . 
K 6 HOH 6   406 202 HOH HOH B . 
K 6 HOH 7   407 404 HOH HOH B . 
K 6 HOH 8   408 453 HOH HOH B . 
K 6 HOH 9   409 344 HOH HOH B . 
K 6 HOH 10  410 426 HOH HOH B . 
K 6 HOH 11  411 469 HOH HOH B . 
K 6 HOH 12  412 32  HOH HOH B . 
K 6 HOH 13  413 217 HOH HOH B . 
K 6 HOH 14  414 416 HOH HOH B . 
K 6 HOH 15  415 584 HOH HOH B . 
K 6 HOH 16  416 105 HOH HOH B . 
K 6 HOH 17  417 477 HOH HOH B . 
K 6 HOH 18  418 192 HOH HOH B . 
K 6 HOH 19  419 399 HOH HOH B . 
K 6 HOH 20  420 172 HOH HOH B . 
K 6 HOH 21  421 420 HOH HOH B . 
K 6 HOH 22  422 474 HOH HOH B . 
K 6 HOH 23  423 207 HOH HOH B . 
K 6 HOH 24  424 454 HOH HOH B . 
K 6 HOH 25  425 23  HOH HOH B . 
K 6 HOH 26  426 222 HOH HOH B . 
K 6 HOH 27  427 132 HOH HOH B . 
K 6 HOH 28  428 360 HOH HOH B . 
K 6 HOH 29  429 229 HOH HOH B . 
K 6 HOH 30  430 544 HOH HOH B . 
K 6 HOH 31  431 558 HOH HOH B . 
K 6 HOH 32  432 126 HOH HOH B . 
K 6 HOH 33  433 370 HOH HOH B . 
K 6 HOH 34  434 167 HOH HOH B . 
K 6 HOH 35  435 185 HOH HOH B . 
K 6 HOH 36  436 481 HOH HOH B . 
K 6 HOH 37  437 8   HOH HOH B . 
K 6 HOH 38  438 479 HOH HOH B . 
K 6 HOH 39  439 411 HOH HOH B . 
K 6 HOH 40  440 321 HOH HOH B . 
K 6 HOH 41  441 560 HOH HOH B . 
K 6 HOH 42  442 147 HOH HOH B . 
K 6 HOH 43  443 89  HOH HOH B . 
K 6 HOH 44  444 324 HOH HOH B . 
K 6 HOH 45  445 402 HOH HOH B . 
K 6 HOH 46  446 96  HOH HOH B . 
K 6 HOH 47  447 86  HOH HOH B . 
K 6 HOH 48  448 43  HOH HOH B . 
K 6 HOH 49  449 111 HOH HOH B . 
K 6 HOH 50  450 205 HOH HOH B . 
K 6 HOH 51  451 78  HOH HOH B . 
K 6 HOH 52  452 409 HOH HOH B . 
K 6 HOH 53  453 21  HOH HOH B . 
K 6 HOH 54  454 434 HOH HOH B . 
K 6 HOH 55  455 397 HOH HOH B . 
K 6 HOH 56  456 294 HOH HOH B . 
K 6 HOH 57  457 55  HOH HOH B . 
K 6 HOH 58  458 125 HOH HOH B . 
K 6 HOH 59  459 239 HOH HOH B . 
K 6 HOH 60  460 152 HOH HOH B . 
K 6 HOH 61  461 187 HOH HOH B . 
K 6 HOH 62  462 181 HOH HOH B . 
K 6 HOH 63  463 278 HOH HOH B . 
K 6 HOH 64  464 87  HOH HOH B . 
K 6 HOH 65  465 283 HOH HOH B . 
K 6 HOH 66  466 73  HOH HOH B . 
K 6 HOH 67  467 70  HOH HOH B . 
K 6 HOH 68  468 525 HOH HOH B . 
K 6 HOH 69  469 24  HOH HOH B . 
K 6 HOH 70  470 588 HOH HOH B . 
K 6 HOH 71  471 56  HOH HOH B . 
K 6 HOH 72  472 323 HOH HOH B . 
K 6 HOH 73  473 550 HOH HOH B . 
K 6 HOH 74  474 18  HOH HOH B . 
K 6 HOH 75  475 166 HOH HOH B . 
K 6 HOH 76  476 510 HOH HOH B . 
K 6 HOH 77  477 534 HOH HOH B . 
K 6 HOH 78  478 257 HOH HOH B . 
K 6 HOH 79  479 199 HOH HOH B . 
K 6 HOH 80  480 398 HOH HOH B . 
K 6 HOH 81  481 261 HOH HOH B . 
K 6 HOH 82  482 4   HOH HOH B . 
K 6 HOH 83  483 555 HOH HOH B . 
K 6 HOH 84  484 20  HOH HOH B . 
K 6 HOH 85  485 357 HOH HOH B . 
K 6 HOH 86  486 169 HOH HOH B . 
K 6 HOH 87  487 17  HOH HOH B . 
K 6 HOH 88  488 179 HOH HOH B . 
K 6 HOH 89  489 27  HOH HOH B . 
K 6 HOH 90  490 26  HOH HOH B . 
K 6 HOH 91  491 178 HOH HOH B . 
K 6 HOH 92  492 538 HOH HOH B . 
K 6 HOH 93  493 490 HOH HOH B . 
K 6 HOH 94  494 250 HOH HOH B . 
K 6 HOH 95  495 15  HOH HOH B . 
K 6 HOH 96  496 565 HOH HOH B . 
K 6 HOH 97  497 14  HOH HOH B . 
K 6 HOH 98  498 130 HOH HOH B . 
K 6 HOH 99  499 295 HOH HOH B . 
K 6 HOH 100 500 107 HOH HOH B . 
K 6 HOH 101 501 586 HOH HOH B . 
K 6 HOH 102 502 90  HOH HOH B . 
K 6 HOH 103 503 224 HOH HOH B . 
K 6 HOH 104 504 151 HOH HOH B . 
K 6 HOH 105 505 94  HOH HOH B . 
K 6 HOH 106 506 582 HOH HOH B . 
K 6 HOH 107 507 177 HOH HOH B . 
K 6 HOH 108 508 65  HOH HOH B . 
K 6 HOH 109 509 566 HOH HOH B . 
K 6 HOH 110 510 553 HOH HOH B . 
K 6 HOH 111 511 79  HOH HOH B . 
K 6 HOH 112 512 162 HOH HOH B . 
K 6 HOH 113 513 436 HOH HOH B . 
K 6 HOH 114 514 110 HOH HOH B . 
K 6 HOH 115 515 158 HOH HOH B . 
K 6 HOH 116 516 249 HOH HOH B . 
K 6 HOH 117 517 573 HOH HOH B . 
K 6 HOH 118 518 542 HOH HOH B . 
K 6 HOH 119 519 103 HOH HOH B . 
K 6 HOH 120 520 572 HOH HOH B . 
K 6 HOH 121 521 353 HOH HOH B . 
K 6 HOH 122 522 503 HOH HOH B . 
K 6 HOH 123 523 31  HOH HOH B . 
K 6 HOH 124 524 12  HOH HOH B . 
K 6 HOH 125 525 112 HOH HOH B . 
K 6 HOH 126 526 225 HOH HOH B . 
K 6 HOH 127 527 80  HOH HOH B . 
K 6 HOH 128 528 576 HOH HOH B . 
K 6 HOH 129 529 561 HOH HOH B . 
K 6 HOH 130 530 144 HOH HOH B . 
K 6 HOH 131 531 400 HOH HOH B . 
K 6 HOH 132 532 232 HOH HOH B . 
K 6 HOH 133 533 483 HOH HOH B . 
K 6 HOH 134 534 476 HOH HOH B . 
K 6 HOH 135 535 34  HOH HOH B . 
K 6 HOH 136 536 305 HOH HOH B . 
K 6 HOH 137 537 149 HOH HOH B . 
K 6 HOH 138 538 340 HOH HOH B . 
K 6 HOH 139 539 120 HOH HOH B . 
K 6 HOH 140 540 95  HOH HOH B . 
K 6 HOH 141 541 93  HOH HOH B . 
K 6 HOH 142 542 123 HOH HOH B . 
K 6 HOH 143 543 266 HOH HOH B . 
K 6 HOH 144 544 146 HOH HOH B . 
K 6 HOH 145 545 258 HOH HOH B . 
K 6 HOH 146 546 75  HOH HOH B . 
K 6 HOH 147 547 102 HOH HOH B . 
K 6 HOH 148 548 306 HOH HOH B . 
K 6 HOH 149 549 356 HOH HOH B . 
K 6 HOH 150 550 531 HOH HOH B . 
K 6 HOH 151 551 343 HOH HOH B . 
K 6 HOH 152 552 223 HOH HOH B . 
K 6 HOH 153 553 473 HOH HOH B . 
K 6 HOH 154 554 430 HOH HOH B . 
K 6 HOH 155 555 53  HOH HOH B . 
K 6 HOH 156 556 536 HOH HOH B . 
K 6 HOH 157 557 551 HOH HOH B . 
K 6 HOH 158 558 475 HOH HOH B . 
K 6 HOH 159 559 143 HOH HOH B . 
K 6 HOH 160 560 417 HOH HOH B . 
K 6 HOH 161 561 58  HOH HOH B . 
K 6 HOH 162 562 39  HOH HOH B . 
K 6 HOH 163 563 47  HOH HOH B . 
K 6 HOH 164 564 247 HOH HOH B . 
K 6 HOH 165 565 549 HOH HOH B . 
K 6 HOH 166 566 256 HOH HOH B . 
K 6 HOH 167 567 62  HOH HOH B . 
K 6 HOH 168 568 478 HOH HOH B . 
K 6 HOH 169 569 175 HOH HOH B . 
K 6 HOH 170 570 176 HOH HOH B . 
K 6 HOH 171 571 154 HOH HOH B . 
K 6 HOH 172 572 159 HOH HOH B . 
K 6 HOH 173 573 338 HOH HOH B . 
K 6 HOH 174 574 546 HOH HOH B . 
K 6 HOH 175 575 597 HOH HOH B . 
K 6 HOH 176 576 514 HOH HOH B . 
K 6 HOH 177 577 9   HOH HOH B . 
K 6 HOH 178 578 396 HOH HOH B . 
K 6 HOH 179 579 548 HOH HOH B . 
K 6 HOH 180 580 337 HOH HOH B . 
K 6 HOH 181 581 76  HOH HOH B . 
K 6 HOH 182 582 100 HOH HOH B . 
K 6 HOH 183 583 157 HOH HOH B . 
K 6 HOH 184 584 499 HOH HOH B . 
K 6 HOH 185 585 221 HOH HOH B . 
K 6 HOH 186 586 528 HOH HOH B . 
K 6 HOH 187 587 480 HOH HOH B . 
K 6 HOH 188 588 49  HOH HOH B . 
K 6 HOH 189 589 228 HOH HOH B . 
K 6 HOH 190 590 170 HOH HOH B . 
K 6 HOH 191 591 442 HOH HOH B . 
K 6 HOH 192 592 241 HOH HOH B . 
K 6 HOH 193 593 329 HOH HOH B . 
K 6 HOH 194 594 269 HOH HOH B . 
K 6 HOH 195 595 182 HOH HOH B . 
K 6 HOH 196 596 485 HOH HOH B . 
K 6 HOH 197 597 349 HOH HOH B . 
K 6 HOH 198 598 326 HOH HOH B . 
K 6 HOH 199 599 309 HOH HOH B . 
K 6 HOH 200 600 85  HOH HOH B . 
K 6 HOH 201 601 489 HOH HOH B . 
K 6 HOH 202 602 507 HOH HOH B . 
K 6 HOH 203 603 198 HOH HOH B . 
K 6 HOH 204 604 407 HOH HOH B . 
K 6 HOH 205 605 84  HOH HOH B . 
K 6 HOH 206 606 244 HOH HOH B . 
K 6 HOH 207 607 336 HOH HOH B . 
K 6 HOH 208 608 341 HOH HOH B . 
K 6 HOH 209 609 293 HOH HOH B . 
K 6 HOH 210 610 352 HOH HOH B . 
K 6 HOH 211 611 208 HOH HOH B . 
K 6 HOH 212 612 571 HOH HOH B . 
K 6 HOH 213 613 590 HOH HOH B . 
K 6 HOH 214 614 351 HOH HOH B . 
K 6 HOH 215 615 535 HOH HOH B . 
K 6 HOH 216 616 371 HOH HOH B . 
K 6 HOH 217 617 456 HOH HOH B . 
K 6 HOH 218 618 518 HOH HOH B . 
K 6 HOH 219 619 455 HOH HOH B . 
K 6 HOH 220 620 168 HOH HOH B . 
K 6 HOH 221 621 265 HOH HOH B . 
K 6 HOH 222 622 428 HOH HOH B . 
K 6 HOH 223 623 493 HOH HOH B . 
K 6 HOH 224 624 348 HOH HOH B . 
K 6 HOH 225 625 437 HOH HOH B . 
K 6 HOH 226 626 272 HOH HOH B . 
K 6 HOH 227 627 71  HOH HOH B . 
K 6 HOH 228 628 127 HOH HOH B . 
K 6 HOH 229 629 543 HOH HOH B . 
K 6 HOH 230 630 339 HOH HOH B . 
K 6 HOH 231 631 585 HOH HOH B . 
K 6 HOH 232 632 415 HOH HOH B . 
K 6 HOH 233 633 559 HOH HOH B . 
K 6 HOH 234 634 260 HOH HOH B . 
K 6 HOH 235 635 498 HOH HOH B . 
K 6 HOH 236 636 408 HOH HOH B . 
K 6 HOH 237 637 252 HOH HOH B . 
K 6 HOH 238 638 575 HOH HOH B . 
K 6 HOH 239 639 141 HOH HOH B . 
K 6 HOH 240 640 567 HOH HOH B . 
K 6 HOH 241 641 281 HOH HOH B . 
K 6 HOH 242 642 522 HOH HOH B . 
K 6 HOH 243 643 520 HOH HOH B . 
K 6 HOH 244 644 497 HOH HOH B . 
K 6 HOH 245 645 552 HOH HOH B . 
K 6 HOH 246 646 482 HOH HOH B . 
K 6 HOH 247 647 557 HOH HOH B . 
K 6 HOH 248 648 592 HOH HOH B . 
K 6 HOH 249 649 195 HOH HOH B . 
K 6 HOH 250 650 501 HOH HOH B . 
K 6 HOH 251 651 504 HOH HOH B . 
K 6 HOH 252 652 303 HOH HOH B . 
K 6 HOH 253 653 346 HOH HOH B . 
K 6 HOH 254 654 161 HOH HOH B . 
K 6 HOH 255 655 286 HOH HOH B . 
K 6 HOH 256 656 285 HOH HOH B . 
K 6 HOH 257 657 246 HOH HOH B . 
K 6 HOH 258 658 511 HOH HOH B . 
K 6 HOH 259 659 513 HOH HOH B . 
K 6 HOH 260 660 502 HOH HOH B . 
K 6 HOH 261 661 142 HOH HOH B . 
K 6 HOH 262 662 423 HOH HOH B . 
K 6 HOH 263 663 211 HOH HOH B . 
K 6 HOH 264 664 598 HOH HOH B . 
K 6 HOH 265 665 537 HOH HOH B . 
K 6 HOH 266 666 188 HOH HOH B . 
K 6 HOH 267 667 274 HOH HOH B . 
K 6 HOH 268 668 523 HOH HOH B . 
K 6 HOH 269 669 554 HOH HOH B . 
K 6 HOH 270 670 545 HOH HOH B . 
K 6 HOH 271 671 527 HOH HOH B . 
K 6 HOH 272 672 366 HOH HOH B . 
K 6 HOH 273 673 465 HOH HOH B . 
K 6 HOH 274 674 596 HOH HOH B . 
K 6 HOH 275 675 594 HOH HOH B . 
K 6 HOH 276 676 113 HOH HOH B . 
K 6 HOH 277 677 579 HOH HOH B . 
K 6 HOH 278 678 331 HOH HOH B . 
K 6 HOH 279 679 273 HOH HOH B . 
K 6 HOH 280 680 369 HOH HOH B . 
K 6 HOH 281 681 516 HOH HOH B . 
K 6 HOH 282 682 425 HOH HOH B . 
K 6 HOH 283 683 578 HOH HOH B . 
K 6 HOH 284 684 280 HOH HOH B . 
K 6 HOH 285 685 135 HOH HOH B . 
K 6 HOH 286 686 492 HOH HOH B . 
K 6 HOH 287 687 302 HOH HOH B . 
K 6 HOH 288 688 506 HOH HOH B . 
K 6 HOH 289 689 363 HOH HOH B . 
K 6 HOH 290 690 484 HOH HOH B . 
K 6 HOH 291 691 562 HOH HOH B . 
K 6 HOH 292 692 372 HOH HOH B . 
K 6 HOH 293 693 515 HOH HOH B . 
K 6 HOH 294 694 268 HOH HOH B . 
K 6 HOH 295 695 591 HOH HOH B . 
K 6 HOH 296 696 530 HOH HOH B . 
K 6 HOH 297 697 418 HOH HOH B . 
K 6 HOH 298 698 438 HOH HOH B . 
K 6 HOH 299 699 406 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD ? A LYS 9   CD 
2  1 Y 1 A LYS 9   ? CE ? A LYS 9   CE 
3  1 Y 1 A LYS 9   ? NZ ? A LYS 9   NZ 
4  1 Y 1 B HIS 4   ? N  ? B HIS 4   N  
5  1 Y 1 B LYS 9   ? CD ? B LYS 9   CD 
6  1 Y 1 B LYS 9   ? CE ? B LYS 9   CE 
7  1 Y 1 B LYS 9   ? NZ ? B LYS 9   NZ 
8  1 Y 1 B LYS 45  ? NZ ? B LYS 45  NZ 
9  1 Y 1 B LYS 158 ? CD ? B LYS 158 CD 
10 1 Y 1 B LYS 158 ? CE ? B LYS 158 CE 
11 1 Y 1 B LYS 158 ? NZ ? B LYS 158 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0189 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.140 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7Q0C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.060 
_cell.length_a_esd                 ? 
_cell.length_b                     41.348 
_cell.length_b_esd                 ? 
_cell.length_c                     72.029 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7Q0C 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   7Q0C 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.08 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.78 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M sodium bicine (pH 9.0), 0.2 M ammonium sulfate and 2M sodium malonate (pH 7.0)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-21 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9755 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9755 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7Q0C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.120 
_reflns.d_resolution_low                               41.35 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     146352 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           81.300 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.800 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.042 
_reflns.pdbx_netI_over_av_sigmaI                       3.400 
_reflns.pdbx_netI_over_sigmaI                          18.900 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.063 
_reflns.pdbx_Rpim_I_all                                0.032 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.122 1.180  ? 6.700  ? ? ? ? 13503 51.400 ? ? ? ? 0.102 ? ? ? ? ? ? ? ? 3.600 0.102 ? ? ? 0.153 0.079 ? 1  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.180 1.250  ? 7.800  ? ? ? ? 19755 79.300 ? ? ? ? 0.090 ? ? ? ? ? ? ? ? 3.700 0.090 ? ? ? 0.134 0.069 ? 2  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.250 1.340  ? 10.000 ? ? ? ? 20127 86.100 ? ? ? ? 0.071 ? ? ? ? ? ? ? ? 3.900 0.071 ? ? ? 0.110 0.055 ? 3  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.340 1.450  ? 13.300 ? ? ? ? 18676 86.100 ? ? ? ? 0.053 ? ? ? ? ? ? ? ? 3.900 0.053 ? ? ? 0.085 0.043 ? 4  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.450 1.590  ? 16.800 ? ? ? ? 17342 86.500 ? ? ? ? 0.040 ? ? ? ? ? ? ? ? 3.900 0.040 ? ? ? 0.067 0.034 ? 5  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.590 1.770  ? 20.200 ? ? ? ? 15765 87.400 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 3.900 0.033 ? ? ? 0.055 0.028 ? 6  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.770 2.050  ? 21.100 ? ? ? ? 14404 90.100 ? ? ? ? 0.029 ? ? ? ? ? ? ? ? 3.900 0.029 ? ? ? 0.046 0.023 ? 7  1 ? ? ? ? ? ? ? ? ? ? 
? 
2.050 2.510  ? 23.200 ? ? ? ? 12165 90.400 ? ? ? ? 0.027 ? ? ? ? ? ? ? ? 3.900 0.027 ? ? ? 0.042 0.021 ? 8  1 ? ? ? ? ? ? ? ? ? ? 
? 
2.510 3.550  ? 11.700 ? ? ? ? 9504  91.300 ? ? ? ? 0.031 ? ? ? ? ? ? ? ? 3.900 0.031 ? ? ? 0.045 0.023 ? 9  1 ? ? ? ? ? ? ? ? ? ? 
? 
3.550 41.348 ? 6.200  ? ? ? ? 5111  89.700 ? ? ? ? 0.061 ? ? ? ? ? ? ? ? 3.800 0.061 ? ? ? 0.087 0.044 ? 10 1 ? ? ? ? ? ? ? ? ? ? 
? 
# 
_refine.aniso_B[1][1]                            1.4700 
_refine.aniso_B[1][2]                            1.0300 
_refine.aniso_B[1][3]                            -0.4100 
_refine.aniso_B[2][2]                            -0.4100 
_refine.aniso_B[2][3]                            0.9600 
_refine.aniso_B[3][3]                            -0.7500 
_refine.B_iso_max                                357.510 
_refine.B_iso_mean                               18.2860 
_refine.B_iso_min                                5.180 
_refine.correlation_coeff_Fo_to_Fc               0.9710 
_refine.correlation_coeff_Fo_to_Fc_free          0.9590 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7Q0C 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.1200 
_refine.ls_d_res_low                             41.3500 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     131858 
_refine.ls_number_reflns_R_free                  14494 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    81.3200 
_refine.ls_percent_reflns_R_free                 9.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1637 
_refine.ls_R_factor_R_free                       0.1937 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1603 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      3HLJ 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0480 
_refine.pdbx_overall_ESU_R_Free                  0.0470 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.1200 
_refine_hist.d_res_low                        41.3500 
_refine_hist.number_atoms_solvent             602 
_refine_hist.number_atoms_total               4739 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       514 
_refine_hist.pdbx_B_iso_mean_ligand           15.64 
_refine_hist.pdbx_B_iso_mean_solvent          30.88 
_refine_hist.pdbx_number_atoms_protein        4079 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.020  0.019  4627 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.532  1.963  6333 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.172  5.000  586  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 39.027 24.977 213  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.895 15.000 770  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 20.670 15.000 16   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.520  0.200  658  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.018  0.021  3656 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 20.997 3.000  4627 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 28.405 5.000  355  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 25.223 5.000  4724 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.1220 
_refine_ls_shell.d_res_low                        1.1520 
_refine_ls_shell.number_reflns_all                5250 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             483 
_refine_ls_shell.number_reflns_R_work             4767 
_refine_ls_shell.percent_reflns_obs               39.4900 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2150 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.2000 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     7Q0C 
_struct.title                        
'Mimic carbonic anhydrase IX in complex with Methyl 2-chloro-4-(cyclohexylsulfanyl)-5-sulfamoylbenzoate' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        7Q0C 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 5 ? 
J N N 6 ? 
K N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7Q0C A 1 ? 260 ? P00918 1 ? 260 ? 1 260 
2 1 7Q0C B 1 ? 260 ? P00918 1 ? 260 ? 1 260 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7Q0C SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1  
1 7Q0C GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2  
1 7Q0C LEU A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3  
1 7Q0C VAL A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 4  
1 7Q0C LEU A 134 ? UNP P00918 VAL 134 'engineered mutation' 134 5  
1 7Q0C ALA A 203 ? UNP P00918 LEU 203 'engineered mutation' 203 6  
2 7Q0C SER B 65  ? UNP P00918 ALA 65  'engineered mutation' 65  7  
2 7Q0C GLN B 67  ? UNP P00918 ASN 67  'engineered mutation' 67  8  
2 7Q0C LEU B 91  ? UNP P00918 ILE 91  'engineered mutation' 91  9  
2 7Q0C VAL B 130 ? UNP P00918 PHE 130 'engineered mutation' 130 10 
2 7Q0C LEU B 134 ? UNP P00918 VAL 134 'engineered mutation' 134 11 
2 7Q0C ALA B 203 ? UNP P00918 LEU 203 'engineered mutation' 203 12 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,J 
2 1 B,G,H,I,K   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ASP A 19  ? HIS A 15  ASP A 19  5 ? 5 
HELX_P HELX_P2  AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3  AA3 LYS A 126 ? GLY A 128 ? LYS A 126 GLY A 128 5 ? 3 
HELX_P HELX_P4  AA4 ASP A 129 ? LEU A 134 ? ASP A 129 LEU A 134 1 ? 6 
HELX_P HELX_P5  AA5 LYS A 153 ? GLY A 155 ? LYS A 153 GLY A 155 5 ? 3 
HELX_P HELX_P6  AA6 LEU A 156 ? ASP A 161 ? LEU A 156 ASP A 161 1 ? 6 
HELX_P HELX_P7  AA7 VAL A 162 ? LYS A 167 ? VAL A 162 LYS A 167 5 ? 6 
HELX_P HELX_P8  AA8 ASP A 179 ? LEU A 184 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P9  AA9 SER A 218 ? ARG A 226 ? SER A 218 ARG A 226 1 ? 9 
HELX_P HELX_P10 AB1 GLY B 12  ? GLU B 14  ? GLY B 12  GLU B 14  5 ? 3 
HELX_P HELX_P11 AB2 HIS B 15  ? PHE B 20  ? HIS B 15  PHE B 20  1 ? 6 
HELX_P HELX_P12 AB3 PRO B 21  ? GLY B 25  ? PRO B 21  GLY B 25  5 ? 5 
HELX_P HELX_P13 AB4 LYS B 126 ? GLY B 128 ? LYS B 126 GLY B 128 5 ? 3 
HELX_P HELX_P14 AB5 ASP B 129 ? LEU B 134 ? ASP B 129 LEU B 134 1 ? 6 
HELX_P HELX_P15 AB6 LYS B 153 ? GLY B 155 ? LYS B 153 GLY B 155 5 ? 3 
HELX_P HELX_P16 AB7 LEU B 156 ? LEU B 163 ? LEU B 156 LEU B 163 1 ? 8 
HELX_P HELX_P17 AB8 ASP B 164 ? LYS B 167 ? ASP B 164 LYS B 167 5 ? 4 
HELX_P HELX_P18 AB9 ASP B 179 ? LEU B 184 ? ASP B 179 LEU B 184 5 ? 6 
HELX_P HELX_P19 AC1 SER B 219 ? ARG B 226 ? SER B 219 ARG B 226 1 ? 8 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc4 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D 7VZ . N1 ? ? A ZN  301 A 7VZ 302 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc5 metalc ? ? B HIS 94  NE2 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 94  B ZN  301 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc6 metalc ? ? B HIS 96  NE2 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc7 metalc ? ? B HIS 119 ND1 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 119 B ZN  301 1_555 ? ? ? ? ? ? ? 1.966 ? ? 
metalc8 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 H 7VZ . N1 ? ? B ZN  301 B 7VZ 302 1_555 ? ? ? ? ? ? ? 1.778 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.5 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 113.1 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.7  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N1  ? D 7VZ .   ? A 7VZ 302 ? 1_555 112.7 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N1  ? D 7VZ .   ? A 7VZ 302 ? 1_555 113.9 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N1  ? D 7VZ .   ? A 7VZ 302 ? 1_555 112.9 ? 
7  NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 103.6 ? 
8  NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 111.8 ? 
9  NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 99.1  ? 
10 NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 N1  ? H 7VZ .   ? B 7VZ 302 ? 1_555 112.5 ? 
11 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 N1  ? H 7VZ .   ? B 7VZ 302 ? 1_555 111.9 ? 
12 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 N1  ? H 7VZ .   ? B 7VZ 302 ? 1_555 116.4 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -1.30 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 9.63  
3 SER 29  B . ? SER 29  B PRO 30  B ? PRO 30  B 1 -0.03 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 9.75  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 256 ALA A 257 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 206 LEU A 211 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 172 ASP A 174 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 215 VAL A 217 
AA4 1  ASP B 32  ? ILE B 33  ? ASP B 32  ILE B 33  
AA4 2  THR B 108 ? VAL B 109 ? THR B 108 VAL B 109 
AA5 1  LYS B 39  ? TYR B 40  ? LYS B 39  TYR B 40  
AA5 2  LYS B 256 ? ALA B 257 ? LYS B 256 ALA B 257 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
AA5 4  VAL B 206 ? LEU B 211 ? VAL B 206 LEU B 211 
AA5 5  LEU B 140 ? GLY B 150 ? LEU B 140 GLY B 150 
AA5 6  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA5 7  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA5 8  PHE B 66  ? GLU B 69  ? PHE B 66  GLU B 69  
AA5 9  ARG B 58  ? ASN B 61  ? ARG B 58  ASN B 61  
AA5 10 SER B 172 ? ASP B 174 ? SER B 172 ASP B 174 
AA6 1  LEU B 47  ? SER B 50  ? LEU B 47  SER B 50  
AA6 2  VAL B 78  ? GLY B 81  ? VAL B 78  GLY B 81  
AA6 3  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA6 4  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA6 5  LEU B 140 ? GLY B 150 ? LEU B 140 GLY B 150 
AA6 6  ILE B 215 ? SER B 218 ? ILE B 215 SER B 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 257 
AA2 2 3  O LYS A 256 ? O LYS A 256 N THR A 192 ? N THR A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O LEU A 211 ? O LEU A 211 N GLY A 144 ? N GLY A 144 
AA2 5 6  O ILE A 145 ? O ILE A 145 N LEU A 118 ? N LEU A 118 
AA2 6 7  O VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
AA2 7 8  O LEU A 91  ? O LEU A 91  N PHE A 70  ? N PHE A 70  
AA2 8 9  O GLU A 69  ? O GLU A 69  N ARG A 58  ? N ARG A 58  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 173 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 145 
AA3 5 6  N PHE A 146 ? N PHE A 146 O ILE A 215 ? O ILE A 215 
AA4 1 2  N ILE B 33  ? N ILE B 33  O THR B 108 ? O THR B 108 
AA5 1 2  N LYS B 39  ? N LYS B 39  O ALA B 257 ? O ALA B 257 
AA5 2 3  O LYS B 256 ? O LYS B 256 N THR B 192 ? N THR B 192 
AA5 3 4  N GLY B 195 ? N GLY B 195 O VAL B 206 ? O VAL B 206 
AA5 4 5  O LEU B 211 ? O LEU B 211 N GLY B 144 ? N GLY B 144 
AA5 5 6  O ILE B 145 ? O ILE B 145 N LEU B 118 ? N LEU B 118 
AA5 6 7  O VAL B 121 ? O VAL B 121 N LEU B 91  ? N LEU B 91  
AA5 7 8  O PHE B 93  ? O PHE B 93  N VAL B 68  ? N VAL B 68  
AA5 8 9  O GLN B 67  ? O GLN B 67  N LEU B 60  ? N LEU B 60  
AA5 9 10 N ILE B 59  ? N ILE B 59  O ALA B 173 ? O ALA B 173 
AA6 1 2  N SER B 50  ? N SER B 50  O VAL B 78  ? O VAL B 78  
AA6 2 3  N LEU B 79  ? N LEU B 79  O TYR B 88  ? O TYR B 88  
AA6 3 4  N LEU B 91  ? N LEU B 91  O VAL B 121 ? O VAL B 121 
AA6 4 5  N LEU B 118 ? N LEU B 118 O ILE B 145 ? O ILE B 145 
AA6 5 6  N PHE B 146 ? N PHE B 146 O ILE B 215 ? O ILE B 215 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    58 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    172 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.97 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PHE 
_pdbx_validate_rmsd_angle.auth_seq_id_1              259 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              260 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              260 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                137.58 
_pdbx_validate_rmsd_angle.angle_target_value         121.70 
_pdbx_validate_rmsd_angle.angle_deviation            15.88 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 27  ? ? -145.24 56.94   
2  1 LEU A 57  ? B -145.37 15.35   
3  1 ARG A 58  ? B 160.21  147.64  
4  1 LYS A 76  ? ? -100.00 -81.27  
5  1 LYS A 111 ? ? 76.41   -2.65   
6  1 PHE A 175 ? ? -165.01 64.26   
7  1 ASN A 243 ? ? -98.76  52.37   
8  1 LYS A 251 ? ? 61.43   -130.57 
9  1 ASN A 252 ? ? -105.22 65.84   
10 1 ASN B 11  ? ? -145.55 12.03   
11 1 ARG B 27  ? ? -142.48 56.50   
12 1 LYS B 76  ? ? -121.60 -75.49  
13 1 LYS B 111 ? ? 81.62   -3.79   
14 1 LYS B 111 ? ? 74.93   -3.79   
15 1 PHE B 175 ? ? -157.86 57.25   
16 1 PHE B 175 ? ? -157.86 63.30   
17 1 GLU B 233 ? ? -22.73  -32.41  
18 1 ASN B 243 ? ? -95.55  47.10   
19 1 LYS B 251 ? ? 52.49   -135.72 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 GLU A 69 ? A -11.60 
2 1 PHE B 66 ? ? 17.64  
3 1 GLU B 69 ? A -20.55 
# 
_pdbx_entry_details.entry_id                 7Q0C 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   Y 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 703 ? 6.23 . 
2 1 O ? B HOH 698 ? 6.83 . 
3 1 O ? B HOH 699 ? 7.34 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
4 1 Y 1 B MET 1 ? B MET 1 
5 1 Y 1 B SER 2 ? B SER 2 
6 1 Y 1 B HIS 3 ? B HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
7VZ CL   CL N N 1   
7VZ C10  C  Y N 2   
7VZ C11  C  Y N 3   
7VZ C14  C  N N 4   
7VZ O16  O  N N 5   
7VZ C17  C  N N 6   
7VZ O15  O  N N 7   
7VZ C9   C  Y N 8   
7VZ C8   C  Y N 9   
7VZ C7   C  Y N 10  
7VZ S4   S  N N 11  
7VZ O6   O  N N 12  
7VZ N1   N  N N 13  
7VZ O5   O  N N 14  
7VZ C12  C  Y N 15  
7VZ S21  S  N N 16  
7VZ C22  C  N N 17  
7VZ C23  C  N N 18  
7VZ C24  C  N N 19  
7VZ C25  C  N N 20  
7VZ C26  C  N N 21  
7VZ C27  C  N N 22  
7VZ H1   H  N N 23  
7VZ H2   H  N N 24  
7VZ H3   H  N N 25  
7VZ H4   H  N N 26  
7VZ H5   H  N N 27  
7VZ H6   H  N N 28  
7VZ H7   H  N N 29  
7VZ H8   H  N N 30  
7VZ H9   H  N N 31  
7VZ H10  H  N N 32  
7VZ H11  H  N N 33  
7VZ H12  H  N N 34  
7VZ H13  H  N N 35  
7VZ H14  H  N N 36  
7VZ H15  H  N N 37  
7VZ H16  H  N N 38  
7VZ H17  H  N N 39  
7VZ H18  H  N N 40  
ACT C    C  N N 41  
ACT O    O  N N 42  
ACT OXT  O  N N 43  
ACT CH3  C  N N 44  
ACT H1   H  N N 45  
ACT H2   H  N N 46  
ACT H3   H  N N 47  
ALA N    N  N N 48  
ALA CA   C  N S 49  
ALA C    C  N N 50  
ALA O    O  N N 51  
ALA CB   C  N N 52  
ALA OXT  O  N N 53  
ALA H    H  N N 54  
ALA H2   H  N N 55  
ALA HA   H  N N 56  
ALA HB1  H  N N 57  
ALA HB2  H  N N 58  
ALA HB3  H  N N 59  
ALA HXT  H  N N 60  
ARG N    N  N N 61  
ARG CA   C  N S 62  
ARG C    C  N N 63  
ARG O    O  N N 64  
ARG CB   C  N N 65  
ARG CG   C  N N 66  
ARG CD   C  N N 67  
ARG NE   N  N N 68  
ARG CZ   C  N N 69  
ARG NH1  N  N N 70  
ARG NH2  N  N N 71  
ARG OXT  O  N N 72  
ARG H    H  N N 73  
ARG H2   H  N N 74  
ARG HA   H  N N 75  
ARG HB2  H  N N 76  
ARG HB3  H  N N 77  
ARG HG2  H  N N 78  
ARG HG3  H  N N 79  
ARG HD2  H  N N 80  
ARG HD3  H  N N 81  
ARG HE   H  N N 82  
ARG HH11 H  N N 83  
ARG HH12 H  N N 84  
ARG HH21 H  N N 85  
ARG HH22 H  N N 86  
ARG HXT  H  N N 87  
ASN N    N  N N 88  
ASN CA   C  N S 89  
ASN C    C  N N 90  
ASN O    O  N N 91  
ASN CB   C  N N 92  
ASN CG   C  N N 93  
ASN OD1  O  N N 94  
ASN ND2  N  N N 95  
ASN OXT  O  N N 96  
ASN H    H  N N 97  
ASN H2   H  N N 98  
ASN HA   H  N N 99  
ASN HB2  H  N N 100 
ASN HB3  H  N N 101 
ASN HD21 H  N N 102 
ASN HD22 H  N N 103 
ASN HXT  H  N N 104 
ASP N    N  N N 105 
ASP CA   C  N S 106 
ASP C    C  N N 107 
ASP O    O  N N 108 
ASP CB   C  N N 109 
ASP CG   C  N N 110 
ASP OD1  O  N N 111 
ASP OD2  O  N N 112 
ASP OXT  O  N N 113 
ASP H    H  N N 114 
ASP H2   H  N N 115 
ASP HA   H  N N 116 
ASP HB2  H  N N 117 
ASP HB3  H  N N 118 
ASP HD2  H  N N 119 
ASP HXT  H  N N 120 
CYS N    N  N N 121 
CYS CA   C  N R 122 
CYS C    C  N N 123 
CYS O    O  N N 124 
CYS CB   C  N N 125 
CYS SG   S  N N 126 
CYS OXT  O  N N 127 
CYS H    H  N N 128 
CYS H2   H  N N 129 
CYS HA   H  N N 130 
CYS HB2  H  N N 131 
CYS HB3  H  N N 132 
CYS HG   H  N N 133 
CYS HXT  H  N N 134 
DMS S    S  N N 135 
DMS O    O  N N 136 
DMS C1   C  N N 137 
DMS C2   C  N N 138 
DMS H11  H  N N 139 
DMS H12  H  N N 140 
DMS H13  H  N N 141 
DMS H21  H  N N 142 
DMS H22  H  N N 143 
DMS H23  H  N N 144 
GLN N    N  N N 145 
GLN CA   C  N S 146 
GLN C    C  N N 147 
GLN O    O  N N 148 
GLN CB   C  N N 149 
GLN CG   C  N N 150 
GLN CD   C  N N 151 
GLN OE1  O  N N 152 
GLN NE2  N  N N 153 
GLN OXT  O  N N 154 
GLN H    H  N N 155 
GLN H2   H  N N 156 
GLN HA   H  N N 157 
GLN HB2  H  N N 158 
GLN HB3  H  N N 159 
GLN HG2  H  N N 160 
GLN HG3  H  N N 161 
GLN HE21 H  N N 162 
GLN HE22 H  N N 163 
GLN HXT  H  N N 164 
GLU N    N  N N 165 
GLU CA   C  N S 166 
GLU C    C  N N 167 
GLU O    O  N N 168 
GLU CB   C  N N 169 
GLU CG   C  N N 170 
GLU CD   C  N N 171 
GLU OE1  O  N N 172 
GLU OE2  O  N N 173 
GLU OXT  O  N N 174 
GLU H    H  N N 175 
GLU H2   H  N N 176 
GLU HA   H  N N 177 
GLU HB2  H  N N 178 
GLU HB3  H  N N 179 
GLU HG2  H  N N 180 
GLU HG3  H  N N 181 
GLU HE2  H  N N 182 
GLU HXT  H  N N 183 
GLY N    N  N N 184 
GLY CA   C  N N 185 
GLY C    C  N N 186 
GLY O    O  N N 187 
GLY OXT  O  N N 188 
GLY H    H  N N 189 
GLY H2   H  N N 190 
GLY HA2  H  N N 191 
GLY HA3  H  N N 192 
GLY HXT  H  N N 193 
HIS N    N  N N 194 
HIS CA   C  N S 195 
HIS C    C  N N 196 
HIS O    O  N N 197 
HIS CB   C  N N 198 
HIS CG   C  Y N 199 
HIS ND1  N  Y N 200 
HIS CD2  C  Y N 201 
HIS CE1  C  Y N 202 
HIS NE2  N  Y N 203 
HIS OXT  O  N N 204 
HIS H    H  N N 205 
HIS H2   H  N N 206 
HIS HA   H  N N 207 
HIS HB2  H  N N 208 
HIS HB3  H  N N 209 
HIS HD1  H  N N 210 
HIS HD2  H  N N 211 
HIS HE1  H  N N 212 
HIS HE2  H  N N 213 
HIS HXT  H  N N 214 
HOH O    O  N N 215 
HOH H1   H  N N 216 
HOH H2   H  N N 217 
ILE N    N  N N 218 
ILE CA   C  N S 219 
ILE C    C  N N 220 
ILE O    O  N N 221 
ILE CB   C  N S 222 
ILE CG1  C  N N 223 
ILE CG2  C  N N 224 
ILE CD1  C  N N 225 
ILE OXT  O  N N 226 
ILE H    H  N N 227 
ILE H2   H  N N 228 
ILE HA   H  N N 229 
ILE HB   H  N N 230 
ILE HG12 H  N N 231 
ILE HG13 H  N N 232 
ILE HG21 H  N N 233 
ILE HG22 H  N N 234 
ILE HG23 H  N N 235 
ILE HD11 H  N N 236 
ILE HD12 H  N N 237 
ILE HD13 H  N N 238 
ILE HXT  H  N N 239 
LEU N    N  N N 240 
LEU CA   C  N S 241 
LEU C    C  N N 242 
LEU O    O  N N 243 
LEU CB   C  N N 244 
LEU CG   C  N N 245 
LEU CD1  C  N N 246 
LEU CD2  C  N N 247 
LEU OXT  O  N N 248 
LEU H    H  N N 249 
LEU H2   H  N N 250 
LEU HA   H  N N 251 
LEU HB2  H  N N 252 
LEU HB3  H  N N 253 
LEU HG   H  N N 254 
LEU HD11 H  N N 255 
LEU HD12 H  N N 256 
LEU HD13 H  N N 257 
LEU HD21 H  N N 258 
LEU HD22 H  N N 259 
LEU HD23 H  N N 260 
LEU HXT  H  N N 261 
LYS N    N  N N 262 
LYS CA   C  N S 263 
LYS C    C  N N 264 
LYS O    O  N N 265 
LYS CB   C  N N 266 
LYS CG   C  N N 267 
LYS CD   C  N N 268 
LYS CE   C  N N 269 
LYS NZ   N  N N 270 
LYS OXT  O  N N 271 
LYS H    H  N N 272 
LYS H2   H  N N 273 
LYS HA   H  N N 274 
LYS HB2  H  N N 275 
LYS HB3  H  N N 276 
LYS HG2  H  N N 277 
LYS HG3  H  N N 278 
LYS HD2  H  N N 279 
LYS HD3  H  N N 280 
LYS HE2  H  N N 281 
LYS HE3  H  N N 282 
LYS HZ1  H  N N 283 
LYS HZ2  H  N N 284 
LYS HZ3  H  N N 285 
LYS HXT  H  N N 286 
MET N    N  N N 287 
MET CA   C  N S 288 
MET C    C  N N 289 
MET O    O  N N 290 
MET CB   C  N N 291 
MET CG   C  N N 292 
MET SD   S  N N 293 
MET CE   C  N N 294 
MET OXT  O  N N 295 
MET H    H  N N 296 
MET H2   H  N N 297 
MET HA   H  N N 298 
MET HB2  H  N N 299 
MET HB3  H  N N 300 
MET HG2  H  N N 301 
MET HG3  H  N N 302 
MET HE1  H  N N 303 
MET HE2  H  N N 304 
MET HE3  H  N N 305 
MET HXT  H  N N 306 
PHE N    N  N N 307 
PHE CA   C  N S 308 
PHE C    C  N N 309 
PHE O    O  N N 310 
PHE CB   C  N N 311 
PHE CG   C  Y N 312 
PHE CD1  C  Y N 313 
PHE CD2  C  Y N 314 
PHE CE1  C  Y N 315 
PHE CE2  C  Y N 316 
PHE CZ   C  Y N 317 
PHE OXT  O  N N 318 
PHE H    H  N N 319 
PHE H2   H  N N 320 
PHE HA   H  N N 321 
PHE HB2  H  N N 322 
PHE HB3  H  N N 323 
PHE HD1  H  N N 324 
PHE HD2  H  N N 325 
PHE HE1  H  N N 326 
PHE HE2  H  N N 327 
PHE HZ   H  N N 328 
PHE HXT  H  N N 329 
PRO N    N  N N 330 
PRO CA   C  N S 331 
PRO C    C  N N 332 
PRO O    O  N N 333 
PRO CB   C  N N 334 
PRO CG   C  N N 335 
PRO CD   C  N N 336 
PRO OXT  O  N N 337 
PRO H    H  N N 338 
PRO HA   H  N N 339 
PRO HB2  H  N N 340 
PRO HB3  H  N N 341 
PRO HG2  H  N N 342 
PRO HG3  H  N N 343 
PRO HD2  H  N N 344 
PRO HD3  H  N N 345 
PRO HXT  H  N N 346 
SER N    N  N N 347 
SER CA   C  N S 348 
SER C    C  N N 349 
SER O    O  N N 350 
SER CB   C  N N 351 
SER OG   O  N N 352 
SER OXT  O  N N 353 
SER H    H  N N 354 
SER H2   H  N N 355 
SER HA   H  N N 356 
SER HB2  H  N N 357 
SER HB3  H  N N 358 
SER HG   H  N N 359 
SER HXT  H  N N 360 
THR N    N  N N 361 
THR CA   C  N S 362 
THR C    C  N N 363 
THR O    O  N N 364 
THR CB   C  N R 365 
THR OG1  O  N N 366 
THR CG2  C  N N 367 
THR OXT  O  N N 368 
THR H    H  N N 369 
THR H2   H  N N 370 
THR HA   H  N N 371 
THR HB   H  N N 372 
THR HG1  H  N N 373 
THR HG21 H  N N 374 
THR HG22 H  N N 375 
THR HG23 H  N N 376 
THR HXT  H  N N 377 
TRP N    N  N N 378 
TRP CA   C  N S 379 
TRP C    C  N N 380 
TRP O    O  N N 381 
TRP CB   C  N N 382 
TRP CG   C  Y N 383 
TRP CD1  C  Y N 384 
TRP CD2  C  Y N 385 
TRP NE1  N  Y N 386 
TRP CE2  C  Y N 387 
TRP CE3  C  Y N 388 
TRP CZ2  C  Y N 389 
TRP CZ3  C  Y N 390 
TRP CH2  C  Y N 391 
TRP OXT  O  N N 392 
TRP H    H  N N 393 
TRP H2   H  N N 394 
TRP HA   H  N N 395 
TRP HB2  H  N N 396 
TRP HB3  H  N N 397 
TRP HD1  H  N N 398 
TRP HE1  H  N N 399 
TRP HE3  H  N N 400 
TRP HZ2  H  N N 401 
TRP HZ3  H  N N 402 
TRP HH2  H  N N 403 
TRP HXT  H  N N 404 
TYR N    N  N N 405 
TYR CA   C  N S 406 
TYR C    C  N N 407 
TYR O    O  N N 408 
TYR CB   C  N N 409 
TYR CG   C  Y N 410 
TYR CD1  C  Y N 411 
TYR CD2  C  Y N 412 
TYR CE1  C  Y N 413 
TYR CE2  C  Y N 414 
TYR CZ   C  Y N 415 
TYR OH   O  N N 416 
TYR OXT  O  N N 417 
TYR H    H  N N 418 
TYR H2   H  N N 419 
TYR HA   H  N N 420 
TYR HB2  H  N N 421 
TYR HB3  H  N N 422 
TYR HD1  H  N N 423 
TYR HD2  H  N N 424 
TYR HE1  H  N N 425 
TYR HE2  H  N N 426 
TYR HH   H  N N 427 
TYR HXT  H  N N 428 
VAL N    N  N N 429 
VAL CA   C  N S 430 
VAL C    C  N N 431 
VAL O    O  N N 432 
VAL CB   C  N N 433 
VAL CG1  C  N N 434 
VAL CG2  C  N N 435 
VAL OXT  O  N N 436 
VAL H    H  N N 437 
VAL H2   H  N N 438 
VAL HA   H  N N 439 
VAL HB   H  N N 440 
VAL HG11 H  N N 441 
VAL HG12 H  N N 442 
VAL HG13 H  N N 443 
VAL HG21 H  N N 444 
VAL HG22 H  N N 445 
VAL HG23 H  N N 446 
VAL HXT  H  N N 447 
ZN  ZN   ZN N N 448 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
7VZ N1  S4   sing N N 1   
7VZ O6  S4   doub N N 2   
7VZ C17 O16  sing N N 3   
7VZ O16 C14  sing N N 4   
7VZ S4  C7   sing N N 5   
7VZ S4  O5   doub N N 6   
7VZ C12 C7   doub Y N 7   
7VZ C12 C11  sing Y N 8   
7VZ C7  C8   sing Y N 9   
7VZ C14 C11  sing N N 10  
7VZ C14 O15  doub N N 11  
7VZ C11 C10  doub Y N 12  
7VZ C8  S21  sing N N 13  
7VZ C8  C9   doub Y N 14  
7VZ C10 C9   sing Y N 15  
7VZ C10 CL   sing N N 16  
7VZ S21 C22  sing N N 17  
7VZ C26 C27  sing N N 18  
7VZ C26 C25  sing N N 19  
7VZ C27 C22  sing N N 20  
7VZ C22 C23  sing N N 21  
7VZ C23 C24  sing N N 22  
7VZ C25 C24  sing N N 23  
7VZ C17 H1   sing N N 24  
7VZ C17 H2   sing N N 25  
7VZ C17 H3   sing N N 26  
7VZ C9  H4   sing N N 27  
7VZ N1  H5   sing N N 28  
7VZ N1  H6   sing N N 29  
7VZ C12 H7   sing N N 30  
7VZ C22 H8   sing N N 31  
7VZ C23 H9   sing N N 32  
7VZ C23 H10  sing N N 33  
7VZ C24 H11  sing N N 34  
7VZ C24 H12  sing N N 35  
7VZ C25 H13  sing N N 36  
7VZ C25 H14  sing N N 37  
7VZ C26 H15  sing N N 38  
7VZ C26 H16  sing N N 39  
7VZ C27 H17  sing N N 40  
7VZ C27 H18  sing N N 41  
ACT C   O    doub N N 42  
ACT C   OXT  sing N N 43  
ACT C   CH3  sing N N 44  
ACT CH3 H1   sing N N 45  
ACT CH3 H2   sing N N 46  
ACT CH3 H3   sing N N 47  
ALA N   CA   sing N N 48  
ALA N   H    sing N N 49  
ALA N   H2   sing N N 50  
ALA CA  C    sing N N 51  
ALA CA  CB   sing N N 52  
ALA CA  HA   sing N N 53  
ALA C   O    doub N N 54  
ALA C   OXT  sing N N 55  
ALA CB  HB1  sing N N 56  
ALA CB  HB2  sing N N 57  
ALA CB  HB3  sing N N 58  
ALA OXT HXT  sing N N 59  
ARG N   CA   sing N N 60  
ARG N   H    sing N N 61  
ARG N   H2   sing N N 62  
ARG CA  C    sing N N 63  
ARG CA  CB   sing N N 64  
ARG CA  HA   sing N N 65  
ARG C   O    doub N N 66  
ARG C   OXT  sing N N 67  
ARG CB  CG   sing N N 68  
ARG CB  HB2  sing N N 69  
ARG CB  HB3  sing N N 70  
ARG CG  CD   sing N N 71  
ARG CG  HG2  sing N N 72  
ARG CG  HG3  sing N N 73  
ARG CD  NE   sing N N 74  
ARG CD  HD2  sing N N 75  
ARG CD  HD3  sing N N 76  
ARG NE  CZ   sing N N 77  
ARG NE  HE   sing N N 78  
ARG CZ  NH1  sing N N 79  
ARG CZ  NH2  doub N N 80  
ARG NH1 HH11 sing N N 81  
ARG NH1 HH12 sing N N 82  
ARG NH2 HH21 sing N N 83  
ARG NH2 HH22 sing N N 84  
ARG OXT HXT  sing N N 85  
ASN N   CA   sing N N 86  
ASN N   H    sing N N 87  
ASN N   H2   sing N N 88  
ASN CA  C    sing N N 89  
ASN CA  CB   sing N N 90  
ASN CA  HA   sing N N 91  
ASN C   O    doub N N 92  
ASN C   OXT  sing N N 93  
ASN CB  CG   sing N N 94  
ASN CB  HB2  sing N N 95  
ASN CB  HB3  sing N N 96  
ASN CG  OD1  doub N N 97  
ASN CG  ND2  sing N N 98  
ASN ND2 HD21 sing N N 99  
ASN ND2 HD22 sing N N 100 
ASN OXT HXT  sing N N 101 
ASP N   CA   sing N N 102 
ASP N   H    sing N N 103 
ASP N   H2   sing N N 104 
ASP CA  C    sing N N 105 
ASP CA  CB   sing N N 106 
ASP CA  HA   sing N N 107 
ASP C   O    doub N N 108 
ASP C   OXT  sing N N 109 
ASP CB  CG   sing N N 110 
ASP CB  HB2  sing N N 111 
ASP CB  HB3  sing N N 112 
ASP CG  OD1  doub N N 113 
ASP CG  OD2  sing N N 114 
ASP OD2 HD2  sing N N 115 
ASP OXT HXT  sing N N 116 
CYS N   CA   sing N N 117 
CYS N   H    sing N N 118 
CYS N   H2   sing N N 119 
CYS CA  C    sing N N 120 
CYS CA  CB   sing N N 121 
CYS CA  HA   sing N N 122 
CYS C   O    doub N N 123 
CYS C   OXT  sing N N 124 
CYS CB  SG   sing N N 125 
CYS CB  HB2  sing N N 126 
CYS CB  HB3  sing N N 127 
CYS SG  HG   sing N N 128 
CYS OXT HXT  sing N N 129 
DMS S   O    doub N N 130 
DMS S   C1   sing N N 131 
DMS S   C2   sing N N 132 
DMS C1  H11  sing N N 133 
DMS C1  H12  sing N N 134 
DMS C1  H13  sing N N 135 
DMS C2  H21  sing N N 136 
DMS C2  H22  sing N N 137 
DMS C2  H23  sing N N 138 
GLN N   CA   sing N N 139 
GLN N   H    sing N N 140 
GLN N   H2   sing N N 141 
GLN CA  C    sing N N 142 
GLN CA  CB   sing N N 143 
GLN CA  HA   sing N N 144 
GLN C   O    doub N N 145 
GLN C   OXT  sing N N 146 
GLN CB  CG   sing N N 147 
GLN CB  HB2  sing N N 148 
GLN CB  HB3  sing N N 149 
GLN CG  CD   sing N N 150 
GLN CG  HG2  sing N N 151 
GLN CG  HG3  sing N N 152 
GLN CD  OE1  doub N N 153 
GLN CD  NE2  sing N N 154 
GLN NE2 HE21 sing N N 155 
GLN NE2 HE22 sing N N 156 
GLN OXT HXT  sing N N 157 
GLU N   CA   sing N N 158 
GLU N   H    sing N N 159 
GLU N   H2   sing N N 160 
GLU CA  C    sing N N 161 
GLU CA  CB   sing N N 162 
GLU CA  HA   sing N N 163 
GLU C   O    doub N N 164 
GLU C   OXT  sing N N 165 
GLU CB  CG   sing N N 166 
GLU CB  HB2  sing N N 167 
GLU CB  HB3  sing N N 168 
GLU CG  CD   sing N N 169 
GLU CG  HG2  sing N N 170 
GLU CG  HG3  sing N N 171 
GLU CD  OE1  doub N N 172 
GLU CD  OE2  sing N N 173 
GLU OE2 HE2  sing N N 174 
GLU OXT HXT  sing N N 175 
GLY N   CA   sing N N 176 
GLY N   H    sing N N 177 
GLY N   H2   sing N N 178 
GLY CA  C    sing N N 179 
GLY CA  HA2  sing N N 180 
GLY CA  HA3  sing N N 181 
GLY C   O    doub N N 182 
GLY C   OXT  sing N N 183 
GLY OXT HXT  sing N N 184 
HIS N   CA   sing N N 185 
HIS N   H    sing N N 186 
HIS N   H2   sing N N 187 
HIS CA  C    sing N N 188 
HIS CA  CB   sing N N 189 
HIS CA  HA   sing N N 190 
HIS C   O    doub N N 191 
HIS C   OXT  sing N N 192 
HIS CB  CG   sing N N 193 
HIS CB  HB2  sing N N 194 
HIS CB  HB3  sing N N 195 
HIS CG  ND1  sing Y N 196 
HIS CG  CD2  doub Y N 197 
HIS ND1 CE1  doub Y N 198 
HIS ND1 HD1  sing N N 199 
HIS CD2 NE2  sing Y N 200 
HIS CD2 HD2  sing N N 201 
HIS CE1 NE2  sing Y N 202 
HIS CE1 HE1  sing N N 203 
HIS NE2 HE2  sing N N 204 
HIS OXT HXT  sing N N 205 
HOH O   H1   sing N N 206 
HOH O   H2   sing N N 207 
ILE N   CA   sing N N 208 
ILE N   H    sing N N 209 
ILE N   H2   sing N N 210 
ILE CA  C    sing N N 211 
ILE CA  CB   sing N N 212 
ILE CA  HA   sing N N 213 
ILE C   O    doub N N 214 
ILE C   OXT  sing N N 215 
ILE CB  CG1  sing N N 216 
ILE CB  CG2  sing N N 217 
ILE CB  HB   sing N N 218 
ILE CG1 CD1  sing N N 219 
ILE CG1 HG12 sing N N 220 
ILE CG1 HG13 sing N N 221 
ILE CG2 HG21 sing N N 222 
ILE CG2 HG22 sing N N 223 
ILE CG2 HG23 sing N N 224 
ILE CD1 HD11 sing N N 225 
ILE CD1 HD12 sing N N 226 
ILE CD1 HD13 sing N N 227 
ILE OXT HXT  sing N N 228 
LEU N   CA   sing N N 229 
LEU N   H    sing N N 230 
LEU N   H2   sing N N 231 
LEU CA  C    sing N N 232 
LEU CA  CB   sing N N 233 
LEU CA  HA   sing N N 234 
LEU C   O    doub N N 235 
LEU C   OXT  sing N N 236 
LEU CB  CG   sing N N 237 
LEU CB  HB2  sing N N 238 
LEU CB  HB3  sing N N 239 
LEU CG  CD1  sing N N 240 
LEU CG  CD2  sing N N 241 
LEU CG  HG   sing N N 242 
LEU CD1 HD11 sing N N 243 
LEU CD1 HD12 sing N N 244 
LEU CD1 HD13 sing N N 245 
LEU CD2 HD21 sing N N 246 
LEU CD2 HD22 sing N N 247 
LEU CD2 HD23 sing N N 248 
LEU OXT HXT  sing N N 249 
LYS N   CA   sing N N 250 
LYS N   H    sing N N 251 
LYS N   H2   sing N N 252 
LYS CA  C    sing N N 253 
LYS CA  CB   sing N N 254 
LYS CA  HA   sing N N 255 
LYS C   O    doub N N 256 
LYS C   OXT  sing N N 257 
LYS CB  CG   sing N N 258 
LYS CB  HB2  sing N N 259 
LYS CB  HB3  sing N N 260 
LYS CG  CD   sing N N 261 
LYS CG  HG2  sing N N 262 
LYS CG  HG3  sing N N 263 
LYS CD  CE   sing N N 264 
LYS CD  HD2  sing N N 265 
LYS CD  HD3  sing N N 266 
LYS CE  NZ   sing N N 267 
LYS CE  HE2  sing N N 268 
LYS CE  HE3  sing N N 269 
LYS NZ  HZ1  sing N N 270 
LYS NZ  HZ2  sing N N 271 
LYS NZ  HZ3  sing N N 272 
LYS OXT HXT  sing N N 273 
MET N   CA   sing N N 274 
MET N   H    sing N N 275 
MET N   H2   sing N N 276 
MET CA  C    sing N N 277 
MET CA  CB   sing N N 278 
MET CA  HA   sing N N 279 
MET C   O    doub N N 280 
MET C   OXT  sing N N 281 
MET CB  CG   sing N N 282 
MET CB  HB2  sing N N 283 
MET CB  HB3  sing N N 284 
MET CG  SD   sing N N 285 
MET CG  HG2  sing N N 286 
MET CG  HG3  sing N N 287 
MET SD  CE   sing N N 288 
MET CE  HE1  sing N N 289 
MET CE  HE2  sing N N 290 
MET CE  HE3  sing N N 291 
MET OXT HXT  sing N N 292 
PHE N   CA   sing N N 293 
PHE N   H    sing N N 294 
PHE N   H2   sing N N 295 
PHE CA  C    sing N N 296 
PHE CA  CB   sing N N 297 
PHE CA  HA   sing N N 298 
PHE C   O    doub N N 299 
PHE C   OXT  sing N N 300 
PHE CB  CG   sing N N 301 
PHE CB  HB2  sing N N 302 
PHE CB  HB3  sing N N 303 
PHE CG  CD1  doub Y N 304 
PHE CG  CD2  sing Y N 305 
PHE CD1 CE1  sing Y N 306 
PHE CD1 HD1  sing N N 307 
PHE CD2 CE2  doub Y N 308 
PHE CD2 HD2  sing N N 309 
PHE CE1 CZ   doub Y N 310 
PHE CE1 HE1  sing N N 311 
PHE CE2 CZ   sing Y N 312 
PHE CE2 HE2  sing N N 313 
PHE CZ  HZ   sing N N 314 
PHE OXT HXT  sing N N 315 
PRO N   CA   sing N N 316 
PRO N   CD   sing N N 317 
PRO N   H    sing N N 318 
PRO CA  C    sing N N 319 
PRO CA  CB   sing N N 320 
PRO CA  HA   sing N N 321 
PRO C   O    doub N N 322 
PRO C   OXT  sing N N 323 
PRO CB  CG   sing N N 324 
PRO CB  HB2  sing N N 325 
PRO CB  HB3  sing N N 326 
PRO CG  CD   sing N N 327 
PRO CG  HG2  sing N N 328 
PRO CG  HG3  sing N N 329 
PRO CD  HD2  sing N N 330 
PRO CD  HD3  sing N N 331 
PRO OXT HXT  sing N N 332 
SER N   CA   sing N N 333 
SER N   H    sing N N 334 
SER N   H2   sing N N 335 
SER CA  C    sing N N 336 
SER CA  CB   sing N N 337 
SER CA  HA   sing N N 338 
SER C   O    doub N N 339 
SER C   OXT  sing N N 340 
SER CB  OG   sing N N 341 
SER CB  HB2  sing N N 342 
SER CB  HB3  sing N N 343 
SER OG  HG   sing N N 344 
SER OXT HXT  sing N N 345 
THR N   CA   sing N N 346 
THR N   H    sing N N 347 
THR N   H2   sing N N 348 
THR CA  C    sing N N 349 
THR CA  CB   sing N N 350 
THR CA  HA   sing N N 351 
THR C   O    doub N N 352 
THR C   OXT  sing N N 353 
THR CB  OG1  sing N N 354 
THR CB  CG2  sing N N 355 
THR CB  HB   sing N N 356 
THR OG1 HG1  sing N N 357 
THR CG2 HG21 sing N N 358 
THR CG2 HG22 sing N N 359 
THR CG2 HG23 sing N N 360 
THR OXT HXT  sing N N 361 
TRP N   CA   sing N N 362 
TRP N   H    sing N N 363 
TRP N   H2   sing N N 364 
TRP CA  C    sing N N 365 
TRP CA  CB   sing N N 366 
TRP CA  HA   sing N N 367 
TRP C   O    doub N N 368 
TRP C   OXT  sing N N 369 
TRP CB  CG   sing N N 370 
TRP CB  HB2  sing N N 371 
TRP CB  HB3  sing N N 372 
TRP CG  CD1  doub Y N 373 
TRP CG  CD2  sing Y N 374 
TRP CD1 NE1  sing Y N 375 
TRP CD1 HD1  sing N N 376 
TRP CD2 CE2  doub Y N 377 
TRP CD2 CE3  sing Y N 378 
TRP NE1 CE2  sing Y N 379 
TRP NE1 HE1  sing N N 380 
TRP CE2 CZ2  sing Y N 381 
TRP CE3 CZ3  doub Y N 382 
TRP CE3 HE3  sing N N 383 
TRP CZ2 CH2  doub Y N 384 
TRP CZ2 HZ2  sing N N 385 
TRP CZ3 CH2  sing Y N 386 
TRP CZ3 HZ3  sing N N 387 
TRP CH2 HH2  sing N N 388 
TRP OXT HXT  sing N N 389 
TYR N   CA   sing N N 390 
TYR N   H    sing N N 391 
TYR N   H2   sing N N 392 
TYR CA  C    sing N N 393 
TYR CA  CB   sing N N 394 
TYR CA  HA   sing N N 395 
TYR C   O    doub N N 396 
TYR C   OXT  sing N N 397 
TYR CB  CG   sing N N 398 
TYR CB  HB2  sing N N 399 
TYR CB  HB3  sing N N 400 
TYR CG  CD1  doub Y N 401 
TYR CG  CD2  sing Y N 402 
TYR CD1 CE1  sing Y N 403 
TYR CD1 HD1  sing N N 404 
TYR CD2 CE2  doub Y N 405 
TYR CD2 HD2  sing N N 406 
TYR CE1 CZ   doub Y N 407 
TYR CE1 HE1  sing N N 408 
TYR CE2 CZ   sing Y N 409 
TYR CE2 HE2  sing N N 410 
TYR CZ  OH   sing N N 411 
TYR OH  HH   sing N N 412 
TYR OXT HXT  sing N N 413 
VAL N   CA   sing N N 414 
VAL N   H    sing N N 415 
VAL N   H2   sing N N 416 
VAL CA  C    sing N N 417 
VAL CA  CB   sing N N 418 
VAL CA  HA   sing N N 419 
VAL C   O    doub N N 420 
VAL C   OXT  sing N N 421 
VAL CB  CG1  sing N N 422 
VAL CB  CG2  sing N N 423 
VAL CB  HB   sing N N 424 
VAL CG1 HG11 sing N N 425 
VAL CG1 HG12 sing N N 426 
VAL CG1 HG13 sing N N 427 
VAL CG2 HG21 sing N N 428 
VAL CG2 HG22 sing N N 429 
VAL CG2 HG23 sing N N 430 
VAL OXT HXT  sing N N 431 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        7VZ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   7VZ 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7Q0C 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.023776 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005992 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024185 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.014317 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? -19.275 3.047   7.954   1.00 55.44  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? -19.934 1.775   7.747   1.00 50.40  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? -19.438 0.872   6.598   1.00 26.03  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? -19.895 -0.256  6.535   1.00 23.44  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? -21.485 1.962   7.766   1.00 60.09  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? -22.171 1.454   6.534   1.00 71.11  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? -22.025 2.051   5.299   1.00 73.71  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? -23.007 0.405   6.347   1.00 79.38  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? -22.742 1.391   4.405   1.00 96.72  ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? -23.347 0.388   5.016   1.00 87.27  ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? -18.426 1.251   5.806   1.00 21.12  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? -17.913 0.288   4.808   1.00 19.10  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? -16.868 -0.532  5.544   1.00 18.52  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? -16.388 -0.105  6.570   1.00 18.79  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? -17.289 0.987   3.606   1.00 18.61  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? -16.099 1.775   3.932   1.00 14.61  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? -16.106 3.097   4.257   1.00 20.77  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? -14.737 1.328   3.948   1.00 14.19  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? -14.825 3.513   4.488   1.00 18.32  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? -13.943 2.465   4.275   1.00 15.74  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? -14.113 0.099   3.634   1.00 13.48  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? -12.552 2.406   4.342   1.00 13.94  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? -12.735 0.023   3.766   1.00 13.31  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? -11.965 1.183   4.083   1.00 14.36  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? -16.624 -1.745  5.045   1.00 15.63  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? -15.520 -2.539  5.565   1.00 17.14  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? -15.195 -3.667  4.590   1.00 14.99  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? -15.266 -3.480  3.371   1.00 15.80  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? -14.956 -4.831  5.214   1.00 16.64  ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? -14.467 -5.996  4.465   1.00 19.71  ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? -15.348 -7.261  4.597   1.00 28.99  ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? -14.995 -8.267  3.957   1.00 38.76  ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? -12.948 -6.281  4.736   1.00 21.79  ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? -12.054 -5.196  4.199   1.00 11.10  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? -11.737 -5.195  2.844   1.00 11.10  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? -11.563 -4.191  5.024   1.00 12.03  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? -10.869 -4.235  2.364   1.00 9.14   ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? -10.720 -3.202  4.546   1.00 12.58  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? -10.353 -3.257  3.213   1.00 9.37   ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -9.553  -2.288  2.739   1.00 10.71  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? -16.508 -7.084  5.235   1.00 29.27  ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? -17.466 -8.164  5.511   1.00 30.88  ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? -18.422 -8.455  4.406   1.00 46.41  ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? -18.488 -7.770  3.415   1.00 42.11  ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? -19.312 -9.432  4.665   1.00 41.08  ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? -20.274 -9.869  3.663   1.00 43.18  ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? -21.275 -8.742  3.346   1.00 33.78  ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? -21.721 -8.592  2.202   1.00 29.24  ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? -20.977 -11.070 4.261   1.00 63.67  ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? -21.830 -11.761 3.212   1.00 47.95  ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? -21.663 -7.952  4.349   1.00 41.67  ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? -22.696 -7.002  3.991   1.00 35.05  ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? -22.171 -5.588  3.790   1.00 80.90  ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? -23.032 -4.734  3.456   1.00 43.24  ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? -23.902 -7.023  4.939   1.00 36.70  ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? -24.513 -8.370  5.092   1.00 17.58  ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? -25.541 -8.843  4.319   1.00 21.33  ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? -24.124 -9.274  5.999   1.00 19.69  ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? -25.758 -10.053 4.808   1.00 18.21  ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? -24.898 -10.356 5.837   1.00 18.15  ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? -20.833 -5.327  3.991   1.00 94.55  ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? -20.311 -3.958  3.861   1.00 34.30  ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? -18.977 -3.971  3.082   1.00 26.15  ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? -18.347 -2.933  3.031   1.00 17.99  ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? -20.004 -3.282  5.198   1.00 40.18  ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? -19.037 -4.033  6.103   1.00 37.84  ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? -18.438 -5.071  5.714   1.00 25.24  ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? -18.685 -3.394  7.235   1.00 24.99  ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? -18.701 -5.122  2.418   1.00 27.71  ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? -17.391 -5.335  1.798   1.00 19.42  ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? -17.384 -4.770  0.393   1.00 15.80  ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? -18.250 -4.039  -0.073  1.00 16.69  ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? -16.281 -5.031  -0.359  1.00 11.36  ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? -16.056 -4.465  -1.707  1.00 13.23  ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? -17.238 -4.491  -2.680  1.00 16.19  ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? -17.290 -3.531  -3.425  1.00 14.12  ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? -14.793 -5.199  -2.250  1.00 14.24  ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? -14.053 -5.482  -0.981  1.00 11.91  ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? -15.099 -5.799  0.094   1.00 13.31  ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? -18.102 -5.545  -2.732  1.00 14.45  ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? -19.220 -5.600  -3.660  1.00 22.07  ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? -20.237 -4.512  -3.307  1.00 17.43  ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? -21.186 -4.362  -4.111  1.00 17.92  ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? -19.784 -7.015  -3.638  1.00 22.23  ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? -18.851 -8.072  -4.242  1.00 25.65  ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? -17.912 -7.643  -5.377  1.00 33.45  ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? -16.630 -7.682  -5.222  1.00 42.88  ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? -18.444 -7.284  -6.448  1.00 50.39  ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? -20.184 -3.958  -2.131  1.00 18.18  ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? -21.214 -2.997  -1.744  1.00 20.73  ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? -20.787 -1.560  -1.876  1.00 134.83 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? -21.578 -0.615  -1.885  1.00 98.11  ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? -21.513 -3.167  -0.287  1.00 22.57  ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? -22.298 -4.409  0.003   1.00 23.02  ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? -23.666 -4.467  -0.071  1.00 22.79  ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? -21.882 -5.657  0.306   1.00 21.92  ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? -24.065 -5.693  0.206   1.00 28.12  ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? -23.008 -6.440  0.419   1.00 24.12  ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? -19.439 -1.351  -1.939  1.00 23.06  ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? -18.882 0.019   -1.931  1.00 46.50  ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? -19.436 1.002   -2.942  1.00 39.60  ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? -19.568 2.165   -2.651  1.00 20.12  ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? -17.350 -0.029  -2.047  1.00 16.23  ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? -16.686 -0.742  -0.893  1.00 13.34  ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? -17.238 -1.156  0.289   1.00 11.22  ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? -15.287 -1.046  -0.814  1.00 11.78  ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? -16.284 -1.734  1.083   1.00 11.74  ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? -15.066 -1.653  0.436   1.00 11.78  ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? -14.192 -0.853  -1.689  1.00 11.84  ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? -13.772 -2.085  0.830   1.00 11.84  ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? -12.921 -1.288  -1.310  1.00 9.67   ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? -12.713 -1.869  -0.062  1.00 10.27  ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? -19.745 0.488   -4.112  1.00 15.96  ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? -20.253 1.365   -5.173  1.00 13.75  ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? -21.585 2.103   -4.794  1.00 18.82  ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? -21.943 3.133   -5.415  1.00 20.99  ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? -20.547 0.543   -6.453  1.00 16.16  ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? -21.745 -0.342  -6.327  1.00 18.63  ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? -22.919 0.120   -6.899  1.00 21.54  ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? -22.021 -1.498  -5.669  1.00 177.43 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? -23.814 -0.838  -6.707  1.00 91.49  ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? -23.354 -1.795  -5.910  1.00 94.90  ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? -22.352 1.580   -3.768  1.00 16.38  ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? -23.603 2.282   -3.396  1.00 15.95  ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? -23.296 3.670   -2.798  1.00 24.04  ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? -23.904 4.782   -3.100  1.00 29.32  ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? -24.418 1.447   -2.409  1.00 15.63  ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? -25.338 0.431   -3.067  1.00 19.23  ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? -25.867 -0.572  -2.056  1.00 20.80  ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? -24.932 -1.762  -1.916  1.00 20.10  ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? -25.231 -2.562  -0.697  1.00 33.16  ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? -22.194 3.745   -2.034  1.00 18.64  ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? -21.799 5.003   -1.374  1.00 17.68  ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? -20.731 5.740   -2.228  1.00 18.49  ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? -20.615 6.936   -2.091  1.00 20.37  ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? -21.225 4.742   0.027   1.00 23.13  ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? -22.232 4.850   1.155   1.00 21.97  ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? -23.312 5.395   0.917   1.00 30.46  ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? -21.948 4.305   2.247   1.00 44.80  ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? -20.040 5.036   -3.112  1.00 18.53  ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? -18.923 5.591   -3.873  1.00 21.98  ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? -19.045 5.041   -5.275  1.00 15.92  ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? -18.400 4.069   -5.611  1.00 14.04  ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? -17.579 5.178   -3.188  1.00 26.97  ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? -17.499 5.612   -1.794  1.00 27.23  ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? -17.203 6.922   -1.523  1.00 25.35  ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? -17.803 4.787   -0.787  1.00 24.80  ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? -17.213 7.361   -0.250  1.00 29.43  ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? -17.807 5.225   0.507   1.00 25.99  ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? -17.494 6.516   0.752   1.00 28.93  ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? -19.912 5.646   -6.128  1.00 18.20  ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? -20.112 5.113   -7.474  1.00 20.44  ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? -18.919 5.003   -8.402  1.00 18.41  ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? -18.958 4.237   -9.381  1.00 21.66  ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? -21.115 6.101   -8.100  1.00 22.99  ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? -21.084 7.328   -7.190  1.00 24.17  ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? -20.764 6.792   -5.788  1.00 19.51  ? 21  PRO A CD  1 
ATOM   158  N  N   A ILE A 1 22  ? -17.854 5.780   -8.071  0.50 15.90  ? 22  ILE A N   1 
ATOM   159  N  N   B ILE A 1 22  ? -17.848 5.767   -8.059  0.50 17.22  ? 22  ILE A N   1 
ATOM   160  C  CA  A ILE A 1 22  ? -16.595 5.664   -8.799  0.50 12.78  ? 22  ILE A CA  1 
ATOM   161  C  CA  B ILE A 1 22  ? -16.591 5.651   -8.789  0.50 14.53  ? 22  ILE A CA  1 
ATOM   162  C  C   A ILE A 1 22  ? -15.986 4.275   -8.647  0.50 13.63  ? 22  ILE A C   1 
ATOM   163  C  C   B ILE A 1 22  ? -15.998 4.259   -8.662  0.50 15.11  ? 22  ILE A C   1 
ATOM   164  O  O   A ILE A 1 22  ? -15.025 3.931   -9.382  0.50 11.45  ? 22  ILE A O   1 
ATOM   165  O  O   B ILE A 1 22  ? -15.059 3.916   -9.418  0.50 12.55  ? 22  ILE A O   1 
ATOM   166  C  CB  A ILE A 1 22  ? -15.645 6.796   -8.340  0.50 12.06  ? 22  ILE A CB  1 
ATOM   167  C  CB  B ILE A 1 22  ? -15.600 6.729   -8.308  0.50 15.23  ? 22  ILE A CB  1 
ATOM   168  C  CG1 A ILE A 1 22  ? -14.479 7.010   -9.317  0.50 10.79  ? 22  ILE A CG1 1 
ATOM   169  C  CG1 B ILE A 1 22  ? -14.705 7.218   -9.454  0.50 12.82  ? 22  ILE A CG1 1 
ATOM   170  C  CG2 A ILE A 1 22  ? -15.113 6.500   -6.931  0.50 10.44  ? 22  ILE A CG2 1 
ATOM   171  C  CG2 B ILE A 1 22  ? -14.747 6.207   -7.139  0.50 17.23  ? 22  ILE A CG2 1 
ATOM   172  C  CD1 A ILE A 1 22  ? -14.821 7.617   -10.652 0.50 15.98  ? 22  ILE A CD1 1 
ATOM   173  C  CD1 B ILE A 1 22  ? -13.720 8.265   -9.020  0.50 12.17  ? 22  ILE A CD1 1 
ATOM   174  N  N   . ALA A 1 23  ? -16.519 3.446   -7.712  1.00 12.30  ? 23  ALA A N   1 
ATOM   175  C  CA  . ALA A 1 23  ? -16.062 2.074   -7.602  1.00 12.11  ? 23  ALA A CA  1 
ATOM   176  C  C   . ALA A 1 23  ? -16.133 1.339   -8.937  1.00 11.71  ? 23  ALA A C   1 
ATOM   177  O  O   . ALA A 1 23  ? -15.452 0.345   -9.130  1.00 11.80  ? 23  ALA A O   1 
ATOM   178  C  CB  . ALA A 1 23  ? -16.913 1.333   -6.533  1.00 18.07  ? 23  ALA A CB  1 
ATOM   179  N  N   . LYS A 1 24  ? -17.077 1.796   -9.815  1.00 13.62  ? 24  LYS A N   1 
ATOM   180  C  CA  . LYS A 1 24  ? -17.248 1.179   -11.128 1.00 13.07  ? 24  LYS A CA  1 
ATOM   181  C  C   . LYS A 1 24  ? -16.656 2.074   -12.225 1.00 14.35  ? 24  LYS A C   1 
ATOM   182  O  O   . LYS A 1 24  ? -16.966 1.910   -13.397 1.00 16.03  ? 24  LYS A O   1 
ATOM   183  C  CB  . LYS A 1 24  ? -18.737 0.897   -11.395 1.00 20.09  ? 24  LYS A CB  1 
ATOM   184  C  CG  . LYS A 1 24  ? -19.383 -0.131  -10.439 1.00 19.76  ? 24  LYS A CG  1 
ATOM   185  C  CD  . LYS A 1 24  ? -20.929 -0.451  -10.835 1.00 42.83  ? 24  LYS A CD  1 
ATOM   186  C  CE  . LYS A 1 24  ? -21.809 -1.197  -9.802  1.00 50.31  ? 24  LYS A CE  1 
ATOM   187  N  NZ  . LYS A 1 24  ? -21.162 -2.527  -9.610  1.00 28.92  ? 24  LYS A NZ  1 
ATOM   188  N  N   . GLY A 1 25  ? -15.621 2.876   -11.857 1.00 13.64  ? 25  GLY A N   1 
ATOM   189  C  CA  . GLY A 1 25  ? -15.061 3.825   -12.803 1.00 13.36  ? 25  GLY A CA  1 
ATOM   190  C  C   . GLY A 1 25  ? -14.060 3.198   -13.764 1.00 12.32  ? 25  GLY A C   1 
ATOM   191  O  O   . GLY A 1 25  ? -13.867 1.983   -13.825 1.00 14.56  ? 25  GLY A O   1 
ATOM   192  N  N   . GLU A 1 26  ? -13.395 4.091   -14.463 1.00 14.14  ? 26  GLU A N   1 
ATOM   193  C  CA  . GLU A 1 26  ? -12.533 3.726   -15.559 1.00 12.98  ? 26  GLU A CA  1 
ATOM   194  C  C   . GLU A 1 26  ? -11.059 3.469   -15.165 1.00 11.46  ? 26  GLU A C   1 
ATOM   195  O  O   . GLU A 1 26  ? -10.264 3.019   -16.023 1.00 12.54  ? 26  GLU A O   1 
ATOM   196  C  CB  . GLU A 1 26  ? -12.564 4.809   -16.641 1.00 19.16  ? 26  GLU A CB  1 
ATOM   197  C  CG  . GLU A 1 26  ? -13.954 5.027   -17.217 1.00 23.07  ? 26  GLU A CG  1 
ATOM   198  C  CD  . GLU A 1 26  ? -14.605 3.795   -17.853 1.00 31.59  ? 26  GLU A CD  1 
ATOM   199  O  OE1 . GLU A 1 26  ? -13.967 3.085   -18.680 1.00 39.94  ? 26  GLU A OE1 1 
ATOM   200  O  OE2 . GLU A 1 26  ? -15.769 3.539   -17.528 1.00 41.66  ? 26  GLU A OE2 1 
ATOM   201  N  N   . ARG A 1 27  ? -10.688 3.780   -13.933 1.00 8.97   ? 27  ARG A N   1 
ATOM   202  C  CA  . ARG A 1 27  ? -9.294  3.583   -13.552 1.00 9.39   ? 27  ARG A CA  1 
ATOM   203  C  C   . ARG A 1 27  ? -9.227  3.155   -12.088 1.00 8.05   ? 27  ARG A C   1 
ATOM   204  O  O   . ARG A 1 27  ? -8.510  3.731   -11.255 1.00 8.11   ? 27  ARG A O   1 
ATOM   205  C  CB  . ARG A 1 27  ? -8.376  4.783   -13.915 1.00 9.86   ? 27  ARG A CB  1 
ATOM   206  C  CG  . ARG A 1 27  ? -8.812  6.096   -13.290 1.00 11.15  ? 27  ARG A CG  1 
ATOM   207  C  CD  . ARG A 1 27  ? -7.856  7.249   -13.453 1.00 11.33  ? 27  ARG A CD  1 
ATOM   208  N  NE  . ARG A 1 27  ? -6.660  7.216   -12.550 1.00 11.07  ? 27  ARG A NE  1 
ATOM   209  C  CZ  . ARG A 1 27  ? -5.692  8.101   -12.523 1.00 8.64   ? 27  ARG A CZ  1 
ATOM   210  N  NH1 . ARG A 1 27  ? -5.706  9.118   -13.373 1.00 10.59  ? 27  ARG A NH1 1 
ATOM   211  N  NH2 . ARG A 1 27  ? -4.710  7.940   -11.672 1.00 10.93  ? 27  ARG A NH2 1 
ATOM   212  N  N   . GLN A 1 28  ? -9.923  2.047   -11.778 1.00 9.13   ? 28  GLN A N   1 
ATOM   213  C  CA  . GLN A 1 28  ? -9.957  1.501   -10.412 1.00 8.73   ? 28  GLN A CA  1 
ATOM   214  C  C   . GLN A 1 28  ? -8.749  0.580   -10.164 1.00 8.10   ? 28  GLN A C   1 
ATOM   215  O  O   . GLN A 1 28  ? -8.320  -0.096  -11.051 1.00 9.04   ? 28  GLN A O   1 
ATOM   216  C  CB  . GLN A 1 28  ? -11.318 0.841   -10.143 1.00 9.88   ? 28  GLN A CB  1 
ATOM   217  C  CG  . GLN A 1 28  ? -12.453 1.896   -10.094 1.00 9.22   ? 28  GLN A CG  1 
ATOM   218  C  CD  . GLN A 1 28  ? -12.373 2.656   -8.784  1.00 7.93   ? 28  GLN A CD  1 
ATOM   219  O  OE1 . GLN A 1 28  ? -12.486 2.109   -7.729  1.00 9.27   ? 28  GLN A OE1 1 
ATOM   220  N  NE2 . GLN A 1 28  ? -11.993 3.968   -8.920  1.00 10.82  ? 28  GLN A NE2 1 
ATOM   221  N  N   . SER A 1 29  ? -8.472  0.448   -8.887  1.00 7.52   ? 29  SER A N   1 
ATOM   222  C  CA  . SER A 1 29  ? -7.378  -0.433  -8.416  1.00 6.77   ? 29  SER A CA  1 
ATOM   223  C  C   . SER A 1 29  ? -7.900  -1.356  -7.316  1.00 5.65   ? 29  SER A C   1 
ATOM   224  O  O   . SER A 1 29  ? -8.880  -0.948  -6.643  1.00 7.48   ? 29  SER A O   1 
ATOM   225  C  CB  . SER A 1 29  ? -6.244  0.409   -7.838  1.00 6.64   ? 29  SER A CB  1 
ATOM   226  O  OG  . SER A 1 29  ? -5.642  1.190   -8.924  1.00 6.68   ? 29  SER A OG  1 
ATOM   227  N  N   . PRO A 1 30  ? -7.290  -2.468  -7.038  1.00 6.64   ? 30  PRO A N   1 
ATOM   228  C  CA  . PRO A 1 30  ? -6.067  -2.995  -7.737  1.00 6.88   ? 30  PRO A CA  1 
ATOM   229  C  C   . PRO A 1 30  ? -6.456  -3.589  -9.066  1.00 7.21   ? 30  PRO A C   1 
ATOM   230  O  O   . PRO A 1 30  ? -7.693  -3.665  -9.452  1.00 8.81   ? 30  PRO A O   1 
ATOM   231  C  CB  . PRO A 1 30  ? -5.569  -4.024  -6.745  1.00 7.30   ? 30  PRO A CB  1 
ATOM   232  C  CG  . PRO A 1 30  ? -6.882  -4.585  -6.199  1.00 7.52   ? 30  PRO A CG  1 
ATOM   233  C  CD  . PRO A 1 30  ? -7.730  -3.395  -6.003  1.00 6.87   ? 30  PRO A CD  1 
ATOM   234  N  N   . VAL A 1 31  ? -5.520  -4.186  -9.786  1.00 6.35   ? 31  VAL A N   1 
ATOM   235  C  CA  . VAL A 1 31  ? -5.683  -4.924  -11.021 1.00 7.59   ? 31  VAL A CA  1 
ATOM   236  C  C   . VAL A 1 31  ? -4.833  -6.164  -10.950 1.00 7.05   ? 31  VAL A C   1 
ATOM   237  O  O   . VAL A 1 31  ? -3.834  -6.210  -10.191 1.00 7.41   ? 31  VAL A O   1 
ATOM   238  C  CB  . VAL A 1 31  ? -5.373  -4.055  -12.283 1.00 6.81   ? 31  VAL A CB  1 
ATOM   239  C  CG1 . VAL A 1 31  ? -6.219  -2.867  -12.351 1.00 7.88   ? 31  VAL A CG1 1 
ATOM   240  C  CG2 . VAL A 1 31  ? -3.906  -3.575  -12.337 1.00 8.09   ? 31  VAL A CG2 1 
ATOM   241  N  N   . ASP A 1 32  ? -5.154  -7.142  -11.810 1.00 7.43   ? 32  ASP A N   1 
ATOM   242  C  CA  . ASP A 1 32  ? -4.223  -8.207  -12.113 1.00 7.49   ? 32  ASP A CA  1 
ATOM   243  C  C   . ASP A 1 32  ? -3.157  -7.706  -13.100 1.00 5.80   ? 32  ASP A C   1 
ATOM   244  O  O   . ASP A 1 32  ? -3.463  -7.054  -14.072 1.00 8.10   ? 32  ASP A O   1 
ATOM   245  C  CB  . ASP A 1 32  ? -4.967  -9.362  -12.741 1.00 8.38   ? 32  ASP A CB  1 
ATOM   246  C  CG  . ASP A 1 32  ? -4.003  -10.520 -13.036 1.00 8.23   ? 32  ASP A CG  1 
ATOM   247  O  OD1 . ASP A 1 32  ? -3.330  -11.018 -12.121 1.00 7.56   ? 32  ASP A OD1 1 
ATOM   248  O  OD2 . ASP A 1 32  ? -3.963  -10.966 -14.272 1.00 10.77  ? 32  ASP A OD2 1 
ATOM   249  N  N   . ILE A 1 33  ? -1.927  -8.024  -12.807 1.00 7.02   ? 33  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 33  ? -0.796  -7.630  -13.673 1.00 8.93   ? 33  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 33  ? -0.474  -8.865  -14.510 1.00 7.96   ? 33  ILE A C   1 
ATOM   252  O  O   . ILE A 1 33  ? 0.024   -9.859  -14.016 1.00 8.11   ? 33  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 33  ? 0.435   -7.217  -12.834 1.00 9.11   ? 33  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 33  ? 0.062   -5.983  -11.999 1.00 10.37  ? 33  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 33  ? 1.617   -6.980  -13.810 1.00 11.25  ? 33  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 33  ? 1.118   -5.696  -10.874 1.00 9.70   ? 33  ILE A CD1 1 
ATOM   257  N  N   A ASP A 1 34  ? -0.948  -8.849  -15.742 0.50 8.95   ? 34  ASP A N   1 
ATOM   258  N  N   B ASP A 1 34  ? -0.720  -8.710  -15.816 0.50 9.31   ? 34  ASP A N   1 
ATOM   259  C  CA  A ASP A 1 34  ? -0.609  -9.925  -16.659 0.50 9.16   ? 34  ASP A CA  1 
ATOM   260  C  CA  B ASP A 1 34  ? -0.494  -9.743  -16.827 0.50 11.60  ? 34  ASP A CA  1 
ATOM   261  C  C   A ASP A 1 34  ? 0.808   -9.620  -17.195 0.50 9.92   ? 34  ASP A C   1 
ATOM   262  C  C   B ASP A 1 34  ? 0.947   -9.556  -17.310 0.50 12.81  ? 34  ASP A C   1 
ATOM   263  O  O   A ASP A 1 34  ? 1.016   -8.662  -17.972 0.50 10.25  ? 34  ASP A O   1 
ATOM   264  O  O   B ASP A 1 34  ? 1.299   -8.622  -18.073 0.50 17.59  ? 34  ASP A O   1 
ATOM   265  C  CB  A ASP A 1 34  ? -1.693  -10.005 -17.719 0.50 11.22  ? 34  ASP A CB  1 
ATOM   266  C  CB  B ASP A 1 34  ? -1.503  -9.663  -17.969 0.50 13.95  ? 34  ASP A CB  1 
ATOM   267  C  CG  A ASP A 1 34  ? -1.464  -11.226 -18.584 0.50 12.95  ? 34  ASP A CG  1 
ATOM   268  C  CG  B ASP A 1 34  ? -1.215  -10.711 -19.049 0.50 16.83  ? 34  ASP A CG  1 
ATOM   269  O  OD1 A ASP A 1 34  ? -1.895  -12.305 -18.158 0.50 15.53  ? 34  ASP A OD1 1 
ATOM   270  O  OD1 B ASP A 1 34  ? -0.033  -11.125 -19.185 0.50 18.62  ? 34  ASP A OD1 1 
ATOM   271  O  OD2 A ASP A 1 34  ? -0.861  -11.110 -19.672 0.50 14.47  ? 34  ASP A OD2 1 
ATOM   272  O  OD2 B ASP A 1 34  ? -2.161  -11.088 -19.782 0.50 19.33  ? 34  ASP A OD2 1 
ATOM   273  N  N   . THR A 1 35  ? 1.808   -10.427 -16.806 1.00 11.32  ? 35  THR A N   1 
ATOM   274  C  CA  . THR A 1 35  ? 3.227   -10.090 -17.019 1.00 14.53  ? 35  THR A CA  1 
ATOM   275  C  C   . THR A 1 35  ? 3.606   -10.224 -18.459 1.00 14.91  ? 35  THR A C   1 
ATOM   276  O  O   . THR A 1 35  ? 4.503   -9.560  -18.912 1.00 20.75  ? 35  THR A O   1 
ATOM   277  C  CB  . THR A 1 35  ? 4.089   -11.016 -16.192 1.00 14.90  ? 35  THR A CB  1 
ATOM   278  O  OG1 . THR A 1 35  ? 4.013   -12.351 -16.662 1.00 16.59  ? 35  THR A OG1 1 
ATOM   279  C  CG2 . THR A 1 35  ? 3.886   -10.891 -14.710 1.00 15.36  ? 35  THR A CG2 1 
ATOM   280  N  N   . HIS A 1 36  ? 2.876   -11.045 -19.213 1.00 15.69  ? 36  HIS A N   1 
ATOM   281  C  CA  . HIS A 1 36  ? 3.187   -11.292 -20.599 1.00 18.58  ? 36  HIS A CA  1 
ATOM   282  C  C   . HIS A 1 36  ? 2.744   -10.096 -21.412 1.00 19.94  ? 36  HIS A C   1 
ATOM   283  O  O   . HIS A 1 36  ? 3.362   -9.803  -22.433 1.00 19.10  ? 36  HIS A O   1 
ATOM   284  C  CB  . HIS A 1 36  ? 2.680   -12.673 -21.039 1.00 21.15  ? 36  HIS A CB  1 
ATOM   285  C  CG  . HIS A 1 36  ? 3.636   -13.736 -20.574 1.00 24.85  ? 36  HIS A CG  1 
ATOM   286  N  ND1 . HIS A 1 36  ? 3.292   -14.657 -19.567 1.00 33.49  ? 36  HIS A ND1 1 
ATOM   287  C  CD2 . HIS A 1 36  ? 4.987   -13.867 -20.826 1.00 20.54  ? 36  HIS A CD2 1 
ATOM   288  C  CE1 . HIS A 1 36  ? 4.364   -15.380 -19.279 1.00 41.70  ? 36  HIS A CE1 1 
ATOM   289  N  NE2 . HIS A 1 36  ? 5.405   -14.939 -20.049 1.00 37.72  ? 36  HIS A NE2 1 
ATOM   290  N  N   . THR A 1 37  ? 1.682   -9.417  -20.952 1.00 16.37  ? 37  THR A N   1 
ATOM   291  C  CA  . THR A 1 37  ? 1.106   -8.268  -21.648 1.00 16.14  ? 37  THR A CA  1 
ATOM   292  C  C   . THR A 1 37  ? 1.693   -6.913  -21.271 1.00 14.57  ? 37  THR A C   1 
ATOM   293  O  O   . THR A 1 37  ? 1.581   -5.970  -22.037 1.00 21.23  ? 37  THR A O   1 
ATOM   294  C  CB  . THR A 1 37  ? -0.400  -8.256  -21.464 1.00 21.83  ? 37  THR A CB  1 
ATOM   295  O  OG1 . THR A 1 37  ? -0.940  -9.514  -21.858 1.00 28.54  ? 37  THR A OG1 1 
ATOM   296  C  CG2 . THR A 1 37  ? -1.157  -7.238  -22.291 1.00 24.88  ? 37  THR A CG2 1 
ATOM   297  N  N   . ALA A 1 38  ? 2.204   -6.789  -20.065 1.00 14.97  ? 38  ALA A N   1 
ATOM   298  C  CA  . ALA A 1 38  ? 2.826   -5.540  -19.679 1.00 13.79  ? 38  ALA A CA  1 
ATOM   299  C  C   . ALA A 1 38  ? 3.996   -5.233  -20.596 1.00 20.57  ? 38  ALA A C   1 
ATOM   300  O  O   . ALA A 1 38  ? 4.779   -6.089  -20.962 1.00 27.82  ? 38  ALA A O   1 
ATOM   301  C  CB  . ALA A 1 38  ? 3.290   -5.625  -18.246 1.00 15.51  ? 38  ALA A CB  1 
ATOM   302  N  N   . LYS A 1 39  ? 4.088   -4.011  -21.080 1.00 20.29  ? 39  LYS A N   1 
ATOM   303  C  CA  . LYS A 1 39  ? 5.178   -3.819  -22.014 1.00 22.80  ? 39  LYS A CA  1 
ATOM   304  C  C   . LYS A 1 39  ? 6.358   -3.107  -21.385 1.00 16.97  ? 39  LYS A C   1 
ATOM   305  O  O   . LYS A 1 39  ? 6.200   -2.123  -20.646 1.00 14.26  ? 39  LYS A O   1 
ATOM   306  C  CB  . LYS A 1 39  ? 4.739   -3.033  -23.229 1.00 30.36  ? 39  LYS A CB  1 
ATOM   307  C  CG  . LYS A 1 39  ? 5.798   -3.019  -24.336 1.00 32.24  ? 39  LYS A CG  1 
ATOM   308  C  CD  . LYS A 1 39  ? 5.226   -2.193  -25.417 1.00 26.54  ? 39  LYS A CD  1 
ATOM   309  C  CE  . LYS A 1 39  ? 6.234   -1.386  -26.169 1.00 31.31  ? 39  LYS A CE  1 
ATOM   310  N  NZ  . LYS A 1 39  ? 6.359   -1.963  -27.517 1.00 35.91  ? 39  LYS A NZ  1 
ATOM   311  N  N   . TYR A 1 40  ? 7.539   -3.607  -21.692 1.00 19.59  ? 40  TYR A N   1 
ATOM   312  C  CA  . TYR A 1 40  ? 8.725   -2.904  -21.254 1.00 15.55  ? 40  TYR A CA  1 
ATOM   313  C  C   . TYR A 1 40  ? 8.792   -1.527  -21.925 1.00 14.97  ? 40  TYR A C   1 
ATOM   314  O  O   . TYR A 1 40  ? 8.626   -1.408  -23.160 1.00 15.73  ? 40  TYR A O   1 
ATOM   315  C  CB  . TYR A 1 40  ? 10.001  -3.699  -21.677 1.00 18.88  ? 40  TYR A CB  1 
ATOM   316  C  CG  . TYR A 1 40  ? 11.280  -2.936  -21.520 1.00 22.47  ? 40  TYR A CG  1 
ATOM   317  C  CD1 . TYR A 1 40  ? 11.653  -2.455  -20.266 1.00 22.41  ? 40  TYR A CD1 1 
ATOM   318  C  CD2 . TYR A 1 40  ? 12.122  -2.719  -22.609 1.00 27.58  ? 40  TYR A CD2 1 
ATOM   319  C  CE1 . TYR A 1 40  ? 12.797  -1.719  -20.070 1.00 26.98  ? 40  TYR A CE1 1 
ATOM   320  C  CE2 . TYR A 1 40  ? 13.293  -1.988  -22.419 1.00 35.63  ? 40  TYR A CE2 1 
ATOM   321  C  CZ  . TYR A 1 40  ? 13.648  -1.529  -21.154 1.00 30.57  ? 40  TYR A CZ  1 
ATOM   322  O  OH  . TYR A 1 40  ? 14.769  -0.794  -20.954 1.00 38.28  ? 40  TYR A OH  1 
ATOM   323  N  N   . ASP A 1 41  ? 8.946   -0.507  -21.118 1.00 12.87  ? 41  ASP A N   1 
ATOM   324  C  CA  . ASP A 1 41  ? 9.056   0.900   -21.532 1.00 14.15  ? 41  ASP A CA  1 
ATOM   325  C  C   . ASP A 1 41  ? 10.429  1.457   -21.280 1.00 15.60  ? 41  ASP A C   1 
ATOM   326  O  O   . ASP A 1 41  ? 10.683  1.854   -20.177 1.00 18.66  ? 41  ASP A O   1 
ATOM   327  C  CB  . ASP A 1 41  ? 7.891   1.698   -20.887 1.00 17.61  ? 41  ASP A CB  1 
ATOM   328  C  CG  . ASP A 1 41  ? 7.860   3.131   -21.389 1.00 21.80  ? 41  ASP A CG  1 
ATOM   329  O  OD1 . ASP A 1 41  ? 8.853   3.615   -21.974 1.00 24.26  ? 41  ASP A OD1 1 
ATOM   330  O  OD2 . ASP A 1 41  ? 6.909   3.806   -21.053 1.00 22.43  ? 41  ASP A OD2 1 
ATOM   331  N  N   . PRO A 1 42  ? 11.302  1.462   -22.300 1.00 20.79  ? 42  PRO A N   1 
ATOM   332  C  CA  . PRO A 1 42  ? 12.723  1.793   -22.113 1.00 25.46  ? 42  PRO A CA  1 
ATOM   333  C  C   . PRO A 1 42  ? 12.894  3.277   -21.711 1.00 26.31  ? 42  PRO A C   1 
ATOM   334  O  O   . PRO A 1 42  ? 13.940  3.699   -21.216 1.00 32.33  ? 42  PRO A O   1 
ATOM   335  C  CB  . PRO A 1 42  ? 13.313  1.493   -23.530 1.00 30.89  ? 42  PRO A CB  1 
ATOM   336  C  CG  . PRO A 1 42  ? 12.160  1.774   -24.469 1.00 32.00  ? 42  PRO A CG  1 
ATOM   337  C  CD  . PRO A 1 42  ? 10.967  1.195   -23.720 1.00 25.60  ? 42  PRO A CD  1 
ATOM   338  N  N   . SER A 1 43  ? 11.813  4.055   -21.916 1.00 22.13  ? 43  SER A N   1 
ATOM   339  C  CA  . SER A 1 43  ? 11.732  5.468   -21.498 1.00 26.34  ? 43  SER A CA  1 
ATOM   340  C  C   . SER A 1 43  ? 11.436  5.733   -20.002 1.00 25.05  ? 43  SER A C   1 
ATOM   341  O  O   . SER A 1 43  ? 11.648  6.857   -19.521 1.00 31.44  ? 43  SER A O   1 
ATOM   342  C  CB  . SER A 1 43  ? 10.782  6.251   -22.373 1.00 27.75  ? 43  SER A CB  1 
ATOM   343  O  OG  . SER A 1 43  ? 9.440   6.048   -22.000 1.00 28.83  ? 43  SER A OG  1 
ATOM   344  N  N   . LEU A 1 44  ? 11.069  4.705   -19.217 1.00 24.55  ? 44  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 44  ? 10.810  4.830   -17.773 1.00 26.56  ? 44  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 44  ? 12.131  4.942   -17.029 1.00 24.41  ? 44  LEU A C   1 
ATOM   347  O  O   . LEU A 1 44  ? 13.160  4.401   -17.451 1.00 32.68  ? 44  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 44  ? 10.090  3.597   -17.267 1.00 20.42  ? 44  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 44  ? 8.598   3.572   -17.505 1.00 17.00  ? 44  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 44  ? 8.156   2.210   -17.019 1.00 16.51  ? 44  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 44  ? 7.863   4.633   -16.690 1.00 16.21  ? 44  LEU A CD2 1 
ATOM   352  N  N   . LYS A 1 45  ? 12.182  5.776   -15.978 1.00 25.72  ? 45  LYS A N   1 
ATOM   353  C  CA  . LYS A 1 45  ? 13.391  6.025   -15.197 1.00 23.93  ? 45  LYS A CA  1 
ATOM   354  C  C   . LYS A 1 45  ? 13.438  5.104   -13.962 1.00 24.36  ? 45  LYS A C   1 
ATOM   355  O  O   . LYS A 1 45  ? 12.435  4.481   -13.604 1.00 22.06  ? 45  LYS A O   1 
ATOM   356  C  CB  . LYS A 1 45  ? 13.419  7.513   -14.943 1.00 25.58  ? 45  LYS A CB  1 
ATOM   357  C  CG  . LYS A 1 45  ? 13.486  8.284   -16.256 1.00 31.42  ? 45  LYS A CG  1 
ATOM   358  C  CD  . LYS A 1 45  ? 12.967  9.706   -16.191 1.00 43.63  ? 45  LYS A CD  1 
ATOM   359  C  CE  . LYS A 1 45  ? 13.907  10.659  -16.899 1.00 61.70  ? 45  LYS A CE  1 
ATOM   360  N  NZ  . LYS A 1 45  ? 14.856  11.258  -15.929 1.00 75.92  ? 45  LYS A NZ  1 
ATOM   361  N  N   . PRO A 1 46  ? 14.683  4.890   -13.455 1.00 26.00  ? 46  PRO A N   1 
ATOM   362  C  CA  . PRO A 1 46  ? 14.706  4.119   -12.228 1.00 22.29  ? 46  PRO A CA  1 
ATOM   363  C  C   . PRO A 1 46  ? 13.930  4.918   -11.194 1.00 21.95  ? 46  PRO A C   1 
ATOM   364  O  O   . PRO A 1 46  ? 13.912  6.135   -11.218 1.00 22.58  ? 46  PRO A O   1 
ATOM   365  C  CB  . PRO A 1 46  ? 16.191  4.107   -11.826 1.00 23.47  ? 46  PRO A CB  1 
ATOM   366  C  CG  . PRO A 1 46  ? 16.921  4.355   -13.082 1.00 89.32  ? 46  PRO A CG  1 
ATOM   367  C  CD  . PRO A 1 46  ? 16.033  5.238   -13.934 1.00 34.74  ? 46  PRO A CD  1 
ATOM   368  N  N   . LEU A 1 47  ? 13.254  4.164   -10.321 1.00 28.01  ? 47  LEU A N   1 
ATOM   369  C  CA  . LEU A 1 47  ? 12.614  4.798   -9.184  1.00 16.52  ? 47  LEU A CA  1 
ATOM   370  C  C   . LEU A 1 47  ? 13.689  5.484   -8.296  1.00 22.45  ? 47  LEU A C   1 
ATOM   371  O  O   . LEU A 1 47  ? 14.774  4.926   -8.056  1.00 22.95  ? 47  LEU A O   1 
ATOM   372  C  CB  . LEU A 1 47  ? 11.822  3.677   -8.500  1.00 26.77  ? 47  LEU A CB  1 
ATOM   373  C  CG  . LEU A 1 47  ? 10.755  4.091   -7.551  1.00 24.96  ? 47  LEU A CG  1 
ATOM   374  C  CD1 . LEU A 1 47  ? 9.603   4.876   -8.306  1.00 32.13  ? 47  LEU A CD1 1 
ATOM   375  C  CD2 . LEU A 1 47  ? 10.247  2.825   -6.845  1.00 146.60 ? 47  LEU A CD2 1 
ATOM   376  N  N   . SER A 1 48  ? 13.418  6.704   -7.826  1.00 20.06  ? 48  SER A N   1 
ATOM   377  C  CA  . SER A 1 48  ? 14.249  7.284   -6.768  1.00 14.15  ? 48  SER A CA  1 
ATOM   378  C  C   . SER A 1 48  ? 13.441  7.226   -5.475  1.00 14.29  ? 48  SER A C   1 
ATOM   379  O  O   . SER A 1 48  ? 12.461  7.967   -5.259  1.00 13.45  ? 48  SER A O   1 
ATOM   380  C  CB  . SER A 1 48  ? 14.643  8.701   -7.100  1.00 15.62  ? 48  SER A CB  1 
ATOM   381  O  OG  . SER A 1 48  ? 15.264  9.287   -5.951  1.00 23.11  ? 48  SER A OG  1 
ATOM   382  N  N   . VAL A 1 49  ? 13.897  6.350   -4.573  1.00 15.13  ? 49  VAL A N   1 
ATOM   383  C  CA  . VAL A 1 49  ? 13.279  6.240   -3.272  1.00 18.46  ? 49  VAL A CA  1 
ATOM   384  C  C   . VAL A 1 49  ? 14.221  6.854   -2.249  1.00 18.22  ? 49  VAL A C   1 
ATOM   385  O  O   . VAL A 1 49  ? 15.302  6.296   -2.031  1.00 23.78  ? 49  VAL A O   1 
ATOM   386  C  CB  . VAL A 1 49  ? 12.943  4.765   -2.909  1.00 23.29  ? 49  VAL A CB  1 
ATOM   387  C  CG1 . VAL A 1 49  ? 12.315  4.570   -1.539  1.00 26.82  ? 49  VAL A CG1 1 
ATOM   388  C  CG2 . VAL A 1 49  ? 12.137  4.040   -3.988  1.00 21.28  ? 49  VAL A CG2 1 
ATOM   389  N  N   . SER A 1 50  ? 13.915  8.053   -1.728  1.00 18.38  ? 50  SER A N   1 
ATOM   390  C  CA  . SER A 1 50  ? 14.848  8.768   -0.860  1.00 21.10  ? 50  SER A CA  1 
ATOM   391  C  C   . SER A 1 50  ? 14.207  8.826   0.511   1.00 21.54  ? 50  SER A C   1 
ATOM   392  O  O   . SER A 1 50  ? 13.554  9.811   0.828   1.00 19.03  ? 50  SER A O   1 
ATOM   393  C  CB  . SER A 1 50  ? 15.042  10.209  -1.291  1.00 25.27  ? 50  SER A CB  1 
ATOM   394  O  OG  . SER A 1 50  ? 15.986  10.271  -2.307  1.00 38.18  ? 50  SER A OG  1 
ATOM   395  N  N   . TYR A 1 51  ? 14.498  7.830   1.312   1.00 25.27  ? 51  TYR A N   1 
ATOM   396  C  CA  . TYR A 1 51  ? 13.969  7.689   2.613   1.00 23.23  ? 51  TYR A CA  1 
ATOM   397  C  C   . TYR A 1 51  ? 14.976  7.924   3.774   1.00 22.88  ? 51  TYR A C   1 
ATOM   398  O  O   . TYR A 1 51  ? 14.615  7.758   4.856   1.00 21.04  ? 51  TYR A O   1 
ATOM   399  C  CB  . TYR A 1 51  ? 13.357  6.291   2.757   1.00 18.04  ? 51  TYR A CB  1 
ATOM   400  C  CG  . TYR A 1 51  ? 12.017  6.011   2.013   1.00 15.51  ? 51  TYR A CG  1 
ATOM   401  C  CD1 . TYR A 1 51  ? 11.329  7.005   1.273   1.00 14.78  ? 51  TYR A CD1 1 
ATOM   402  C  CD2 . TYR A 1 51  ? 11.483  4.732   2.042   1.00 14.32  ? 51  TYR A CD2 1 
ATOM   403  C  CE1 . TYR A 1 51  ? 10.120  6.679   0.634   1.00 13.09  ? 51  TYR A CE1 1 
ATOM   404  C  CE2 . TYR A 1 51  ? 10.308  4.408   1.392   1.00 12.12  ? 51  TYR A CE2 1 
ATOM   405  C  CZ  . TYR A 1 51  ? 9.629   5.385   0.678   1.00 12.51  ? 51  TYR A CZ  1 
ATOM   406  O  OH  . TYR A 1 51  ? 8.473   5.059   0.051   1.00 12.74  ? 51  TYR A OH  1 
ATOM   407  N  N   . ASP A 1 52  ? 16.189  8.378   3.496   1.00 32.57  ? 52  ASP A N   1 
ATOM   408  C  CA  . ASP A 1 52  ? 17.203  8.617   4.522   1.00 29.89  ? 52  ASP A CA  1 
ATOM   409  C  C   . ASP A 1 52  ? 16.709  9.507   5.672   1.00 28.54  ? 52  ASP A C   1 
ATOM   410  O  O   . ASP A 1 52  ? 17.085  9.244   6.816   1.00 35.38  ? 52  ASP A O   1 
ATOM   411  C  CB  . ASP A 1 52  ? 18.612  8.892   3.975   1.00 43.67  ? 52  ASP A CB  1 
ATOM   412  C  CG  . ASP A 1 52  ? 18.848  10.270  3.363   1.00 50.49  ? 52  ASP A CG  1 
ATOM   413  O  OD1 . ASP A 1 52  ? 18.103  10.631  2.422   1.00 57.47  ? 52  ASP A OD1 1 
ATOM   414  O  OD2 . ASP A 1 52  ? 19.827  10.949  3.791   1.00 83.53  ? 52  ASP A OD2 1 
ATOM   415  N  N   . GLN A 1 53  ? 15.929  10.551  5.398   1.00 28.56  ? 53  GLN A N   1 
ATOM   416  C  CA  . GLN A 1 53  ? 15.507  11.461  6.473   1.00 31.00  ? 53  GLN A CA  1 
ATOM   417  C  C   . GLN A 1 53  ? 14.055  11.270  6.941   1.00 23.44  ? 53  GLN A C   1 
ATOM   418  O  O   . GLN A 1 53  ? 13.472  12.165  7.533   1.00 26.73  ? 53  GLN A O   1 
ATOM   419  C  CB  . GLN A 1 53  ? 15.602  12.901  5.970   1.00 53.85  ? 53  GLN A CB  1 
ATOM   420  C  CG  . GLN A 1 53  ? 17.052  13.367  5.731   1.00 52.16  ? 53  GLN A CG  1 
ATOM   421  C  CD  . GLN A 1 53  ? 17.966  13.412  6.943   1.00 70.47  ? 53  GLN A CD  1 
ATOM   422  O  OE1 . GLN A 1 53  ? 17.526  13.594  8.113   1.00 81.43  ? 53  GLN A OE1 1 
ATOM   423  N  NE2 . GLN A 1 53  ? 19.276  13.220  6.658   1.00 71.70  ? 53  GLN A NE2 1 
ATOM   424  N  N   . ALA A 1 54  ? 13.496  10.086  6.747   1.00 25.33  ? 54  ALA A N   1 
ATOM   425  C  CA  . ALA A 1 54  ? 12.121  9.841   7.154   1.00 20.96  ? 54  ALA A CA  1 
ATOM   426  C  C   . ALA A 1 54  ? 11.910  9.982   8.672   1.00 21.31  ? 54  ALA A C   1 
ATOM   427  O  O   . ALA A 1 54  ? 12.787  9.620   9.488   1.00 22.86  ? 54  ALA A O   1 
ATOM   428  C  CB  . ALA A 1 54  ? 11.751  8.463   6.665   1.00 22.08  ? 54  ALA A CB  1 
ATOM   429  N  N   . THR A 1 55  ? 10.817  10.662  9.027   1.00 18.73  ? 55  THR A N   1 
ATOM   430  C  CA  . THR A 1 55  ? 10.445  10.835  10.425  1.00 18.47  ? 55  THR A CA  1 
ATOM   431  C  C   . THR A 1 55  ? 9.112   10.147  10.652  1.00 18.85  ? 55  THR A C   1 
ATOM   432  O  O   . THR A 1 55  ? 8.068   10.760  10.397  1.00 20.43  ? 55  THR A O   1 
ATOM   433  C  CB  . THR A 1 55  ? 10.261  12.293  10.867  1.00 26.72  ? 55  THR A CB  1 
ATOM   434  O  OG1 . THR A 1 55  ? 11.537  12.919  10.801  1.00 26.47  ? 55  THR A OG1 1 
ATOM   435  C  CG2 . THR A 1 55  ? 9.836   12.360  12.330  1.00 29.88  ? 55  THR A CG2 1 
ATOM   436  N  N   . SER A 1 56  ? 9.186   8.926   11.169  1.00 23.50  ? 56  SER A N   1 
ATOM   437  C  CA  . SER A 1 56  ? 7.956   8.245   11.533  1.00 22.70  ? 56  SER A CA  1 
ATOM   438  C  C   . SER A 1 56  ? 7.513   8.943   12.813  1.00 24.82  ? 56  SER A C   1 
ATOM   439  O  O   . SER A 1 56  ? 8.312   9.396   13.622  1.00 29.13  ? 56  SER A O   1 
ATOM   440  C  CB  . SER A 1 56  ? 8.085   6.734   11.678  1.00 26.65  ? 56  SER A CB  1 
ATOM   441  O  OG  . SER A 1 56  ? 8.959   6.458   12.796  1.00 23.96  ? 56  SER A OG  1 
ATOM   442  N  N   A LEU A 1 57  ? 6.220   9.120   12.943  0.50 20.76  ? 57  LEU A N   1 
ATOM   443  N  N   B LEU A 1 57  ? 6.191   9.023   12.966  0.50 22.07  ? 57  LEU A N   1 
ATOM   444  C  CA  A LEU A 1 57  ? 5.797   9.869   14.096  0.50 18.52  ? 57  LEU A CA  1 
ATOM   445  C  CA  B LEU A 1 57  ? 5.637   9.822   14.039  0.50 25.15  ? 57  LEU A CA  1 
ATOM   446  C  C   A LEU A 1 57  ? 5.152   8.840   14.953  0.50 17.04  ? 57  LEU A C   1 
ATOM   447  C  C   B LEU A 1 57  ? 4.373   9.210   14.598  0.50 22.36  ? 57  LEU A C   1 
ATOM   448  O  O   A LEU A 1 57  ? 5.255   8.784   16.174  0.50 12.11  ? 57  LEU A O   1 
ATOM   449  O  O   B LEU A 1 57  ? 3.568   9.922   15.215  0.50 20.39  ? 57  LEU A O   1 
ATOM   450  C  CB  A LEU A 1 57  ? 4.667   10.799  13.650  0.50 21.76  ? 57  LEU A CB  1 
ATOM   451  C  CB  B LEU A 1 57  ? 5.323   11.229  13.514  0.50 29.70  ? 57  LEU A CB  1 
ATOM   452  C  CG  A LEU A 1 57  ? 5.128   12.220  13.307  0.50 24.27  ? 57  LEU A CG  1 
ATOM   453  C  CG  B LEU A 1 57  ? 4.053   11.517  12.698  0.50 30.84  ? 57  LEU A CG  1 
ATOM   454  C  CD1 A LEU A 1 57  ? 6.494   12.204  12.658  0.50 31.09  ? 57  LEU A CD1 1 
ATOM   455  C  CD1 B LEU A 1 57  ? 2.763   10.901  13.259  0.50 33.79  ? 57  LEU A CD1 1 
ATOM   456  C  CD2 A LEU A 1 57  ? 4.129   13.026  12.507  0.50 25.01  ? 57  LEU A CD2 1 
ATOM   457  C  CD2 B LEU A 1 57  ? 3.910   13.027  12.542  0.50 27.93  ? 57  LEU A CD2 1 
ATOM   458  N  N   A ARG A 1 58  ? 4.276   8.091   14.253  0.50 20.53  ? 58  ARG A N   1 
ATOM   459  N  N   B ARG A 1 58  ? 4.046   7.924   14.331  0.50 19.14  ? 58  ARG A N   1 
ATOM   460  C  CA  A ARG A 1 58  ? 3.201   7.343   14.924  0.50 15.14  ? 58  ARG A CA  1 
ATOM   461  C  CA  B ARG A 1 58  ? 2.827   7.419   14.995  0.50 18.22  ? 58  ARG A CA  1 
ATOM   462  C  C   A ARG A 1 58  ? 2.844   6.104   14.120  0.50 8.95   ? 58  ARG A C   1 
ATOM   463  C  C   B ARG A 1 58  ? 2.149   6.146   14.373  0.50 15.72  ? 58  ARG A C   1 
ATOM   464  O  O   A ARG A 1 58  ? 2.986   6.049   12.912  0.50 10.58  ? 58  ARG A O   1 
ATOM   465  O  O   B ARG A 1 58  ? 2.144   5.959   13.173  0.50 15.53  ? 58  ARG A O   1 
ATOM   466  C  CB  A ARG A 1 58  ? 1.924   8.225   14.921  0.50 18.31  ? 58  ARG A CB  1 
ATOM   467  C  CB  B ARG A 1 58  ? 1.887   8.604   15.252  0.50 20.49  ? 58  ARG A CB  1 
ATOM   468  C  CG  A ARG A 1 58  ? 0.945   7.853   16.002  0.50 11.40  ? 58  ARG A CG  1 
ATOM   469  C  CG  B ARG A 1 58  ? 0.824   8.337   16.303  0.50 31.12  ? 58  ARG A CG  1 
ATOM   470  C  CD  A ARG A 1 58  ? -0.210  8.805   16.278  0.50 12.09  ? 58  ARG A CD  1 
ATOM   471  C  CD  B ARG A 1 58  ? -0.024  9.513   16.853  0.50 18.15  ? 58  ARG A CD  1 
ATOM   472  N  NE  A ARG A 1 58  ? -0.980  8.941   15.084  0.50 10.00  ? 58  ARG A NE  1 
ATOM   473  N  NE  B ARG A 1 58  ? -0.981  9.026   17.819  0.50 16.15  ? 58  ARG A NE  1 
ATOM   474  C  CZ  A ARG A 1 58  ? -2.283  9.197   15.054  0.50 10.64  ? 58  ARG A CZ  1 
ATOM   475  C  CZ  B ARG A 1 58  ? -0.767  8.975   19.129  0.50 12.64  ? 58  ARG A CZ  1 
ATOM   476  N  NH1 A ARG A 1 58  ? -2.955  9.344   16.183  0.50 10.24  ? 58  ARG A NH1 1 
ATOM   477  N  NH1 B ARG A 1 58  ? 0.385   9.387   19.628  0.50 17.23  ? 58  ARG A NH1 1 
ATOM   478  N  NH2 A ARG A 1 58  ? -2.909  9.305   13.896  0.50 9.42   ? 58  ARG A NH2 1 
ATOM   479  N  NH2 B ARG A 1 58  ? -1.706  8.513   19.935  0.50 22.37  ? 58  ARG A NH2 1 
ATOM   480  N  N   A ILE A 1 59  ? 2.329   5.101   14.849  0.50 7.93   ? 59  ILE A N   1 
ATOM   481  N  N   B ILE A 1 59  ? 1.507   5.248   15.138  0.50 15.49  ? 59  ILE A N   1 
ATOM   482  C  CA  A ILE A 1 59  ? 1.694   3.954   14.227  0.50 9.71   ? 59  ILE A CA  1 
ATOM   483  C  CA  B ILE A 1 59  ? 0.942   4.072   14.504  0.50 16.03  ? 59  ILE A CA  1 
ATOM   484  C  C   A ILE A 1 59  ? 0.254   3.948   14.807  0.50 13.97  ? 59  ILE A C   1 
ATOM   485  C  C   B ILE A 1 59  ? -0.460  4.045   14.931  0.50 14.83  ? 59  ILE A C   1 
ATOM   486  O  O   A ILE A 1 59  ? 0.063   4.379   15.966  0.50 71.84  ? 59  ILE A O   1 
ATOM   487  O  O   B ILE A 1 59  ? -0.828  4.099   16.122  0.50 17.40  ? 59  ILE A O   1 
ATOM   488  C  CB  A ILE A 1 59  ? 2.406   2.629   14.525  0.50 9.27   ? 59  ILE A CB  1 
ATOM   489  C  CB  B ILE A 1 59  ? 1.423   2.670   14.846  0.50 13.45  ? 59  ILE A CB  1 
ATOM   490  C  CG1 A ILE A 1 59  ? 1.781   1.478   13.741  0.50 9.40   ? 59  ILE A CG1 1 
ATOM   491  C  CG1 B ILE A 1 59  ? 0.723   1.584   13.999  0.50 9.23   ? 59  ILE A CG1 1 
ATOM   492  C  CG2 A ILE A 1 59  ? 2.419   2.348   16.019  0.50 10.93  ? 59  ILE A CG2 1 
ATOM   493  C  CG2 B ILE A 1 59  ? 1.254   2.398   16.348  0.50 10.41  ? 59  ILE A CG2 1 
ATOM   494  C  CD1 A ILE A 1 59  ? 2.611   0.239   13.790  0.50 8.29   ? 59  ILE A CD1 1 
ATOM   495  C  CD1 B ILE A 1 59  ? 1.453   0.263   14.105  0.50 11.01  ? 59  ILE A CD1 1 
ATOM   496  N  N   A LEU A 1 60  ? -0.711  3.441   14.023  0.50 15.61  ? 60  LEU A N   1 
ATOM   497  N  N   B LEU A 1 60  ? -1.165  4.049   13.851  0.50 16.74  ? 60  LEU A N   1 
ATOM   498  C  CA  A LEU A 1 60  ? -2.152  3.582   14.300  0.50 8.45   ? 60  LEU A CA  1 
ATOM   499  C  CA  B LEU A 1 60  ? -2.541  3.878   14.044  0.50 15.39  ? 60  LEU A CA  1 
ATOM   500  C  C   A LEU A 1 60  ? -3.148  2.469   13.783  0.50 12.63  ? 60  LEU A C   1 
ATOM   501  C  C   B LEU A 1 60  ? -3.135  2.699   13.273  0.50 73.01  ? 60  LEU A C   1 
ATOM   502  O  O   A LEU A 1 60  ? -3.040  2.138   12.600  0.50 12.84  ? 60  LEU A O   1 
ATOM   503  O  O   B LEU A 1 60  ? -2.718  2.371   12.080  0.50 73.14  ? 60  LEU A O   1 
ATOM   504  C  CB  A LEU A 1 60  ? -2.646  4.930   13.721  0.50 15.39  ? 60  LEU A CB  1 
ATOM   505  C  CB  B LEU A 1 60  ? -3.345  5.134   13.649  0.50 21.10  ? 60  LEU A CB  1 
ATOM   506  C  CG  A LEU A 1 60  ? -4.198  5.075   13.823  0.50 24.66  ? 60  LEU A CG  1 
ATOM   507  C  CG  B LEU A 1 60  ? -4.888  5.083   13.716  0.50 16.31  ? 60  LEU A CG  1 
ATOM   508  C  CD1 A LEU A 1 60  ? -4.686  5.669   15.195  0.50 16.01  ? 60  LEU A CD1 1 
ATOM   509  C  CD1 B LEU A 1 60  ? -5.479  5.300   15.131  0.50 18.24  ? 60  LEU A CD1 1 
ATOM   510  C  CD2 A LEU A 1 60  ? -4.667  5.929   12.636  0.50 24.21  ? 60  LEU A CD2 1 
ATOM   511  C  CD2 B LEU A 1 60  ? -5.467  6.199   12.824  0.50 20.22  ? 60  LEU A CD2 1 
ATOM   512  N  N   A ASN A 1 61  ? -4.242  1.967   14.519  0.50 13.75  ? 61  ASN A N   1 
ATOM   513  N  N   B ASN A 1 61  ? -4.046  2.136   14.049  0.50 29.51  ? 61  ASN A N   1 
ATOM   514  C  CA  A ASN A 1 61  ? -5.343  0.994   14.115  0.50 12.90  ? 61  ASN A CA  1 
ATOM   515  C  CA  B ASN A 1 61  ? -4.942  1.066   13.778  0.50 18.81  ? 61  ASN A CA  1 
ATOM   516  C  C   A ASN A 1 61  ? -6.628  1.694   13.614  0.50 15.99  ? 61  ASN A C   1 
ATOM   517  C  C   B ASN A 1 61  ? -6.211  1.867   13.499  0.50 13.86  ? 61  ASN A C   1 
ATOM   518  O  O   A ASN A 1 61  ? -7.555  2.085   14.400  0.50 15.78  ? 61  ASN A O   1 
ATOM   519  O  O   B ASN A 1 61  ? -6.679  2.607   14.386  0.50 12.98  ? 61  ASN A O   1 
ATOM   520  C  CB  A ASN A 1 61  ? -5.658  0.001   15.237  0.50 14.88  ? 61  ASN A CB  1 
ATOM   521  C  CB  B ASN A 1 61  ? -5.102  0.133   14.980  0.50 13.59  ? 61  ASN A CB  1 
ATOM   522  C  CG  A ASN A 1 61  ? -6.626  -1.083  14.813  0.50 13.29  ? 61  ASN A CG  1 
ATOM   523  C  CG  B ASN A 1 61  ? -6.236  -0.855  14.814  0.50 9.80   ? 61  ASN A CG  1 
ATOM   524  O  OD1 A ASN A 1 61  ? -7.443  -0.877  13.918  0.50 13.25  ? 61  ASN A OD1 1 
ATOM   525  O  OD1 B ASN A 1 61  ? -7.179  -0.605  14.066  0.50 40.27  ? 61  ASN A OD1 1 
ATOM   526  N  ND2 A ASN A 1 61  ? -6.544  -2.240  15.450  0.50 11.92  ? 61  ASN A ND2 1 
ATOM   527  N  ND2 B ASN A 1 61  ? -6.155  -1.980  15.505  0.50 13.79  ? 61  ASN A ND2 1 
ATOM   528  N  N   . ASN A 1 62  ? -6.711  1.801   12.273  1.00 16.80  ? 62  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 62  ? -7.700  2.719   11.741  1.00 21.62  ? 62  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 62  ? -9.028  1.988   11.585  1.00 18.99  ? 62  ASN A C   1 
ATOM   531  O  O   . ASN A 1 62  ? -10.016 2.530   11.029  1.00 24.25  ? 62  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 62  ? -7.228  3.396   10.448  1.00 21.49  ? 62  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 62  ? -7.024  2.399   9.330   1.00 19.42  ? 62  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 62  ? -7.721  1.394   9.271   1.00 15.90  ? 62  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 62  ? -6.031  2.629   8.503   1.00 18.69  ? 62  ASN A ND2 1 
ATOM   536  N  N   . GLY A 1 63  ? -9.062  0.735   12.053  1.00 21.08  ? 63  GLY A N   1 
ATOM   537  C  CA  . GLY A 1 63  ? -10.266 -0.043  11.956  1.00 18.40  ? 63  GLY A CA  1 
ATOM   538  C  C   . GLY A 1 63  ? -10.334 -0.861  10.659  1.00 17.83  ? 63  GLY A C   1 
ATOM   539  O  O   . GLY A 1 63  ? -11.231 -1.689  10.534  1.00 16.47  ? 63  GLY A O   1 
ATOM   540  N  N   . HIS A 1 64  ? -9.437  -0.627  9.709   1.00 13.62  ? 64  HIS A N   1 
ATOM   541  C  CA  . HIS A 1 64  ? -9.377  -1.374  8.437   1.00 13.95  ? 64  HIS A CA  1 
ATOM   542  C  C   . HIS A 1 64  ? -8.048  -2.077  8.289   1.00 12.70  ? 64  HIS A C   1 
ATOM   543  O  O   . HIS A 1 64  ? -7.998  -3.216  7.796   1.00 13.95  ? 64  HIS A O   1 
ATOM   544  C  CB  . HIS A 1 64  ? -9.603  -0.416  7.285   1.00 14.18  ? 64  HIS A CB  1 
ATOM   545  C  CG  . HIS A 1 64  ? -10.866 0.377   7.394   1.00 14.73  ? 64  HIS A CG  1 
ATOM   546  N  ND1 . HIS A 1 64  ? -12.105 -0.216  7.323   1.00 19.18  ? 64  HIS A ND1 1 
ATOM   547  C  CD2 . HIS A 1 64  ? -11.110 1.677   7.665   1.00 17.25  ? 64  HIS A CD2 1 
ATOM   548  C  CE1 . HIS A 1 64  ? -13.069 0.686   7.461   1.00 20.88  ? 64  HIS A CE1 1 
ATOM   549  N  NE2 . HIS A 1 64  ? -12.478 1.840   7.712   1.00 22.17  ? 64  HIS A NE2 1 
ATOM   550  N  N   . SER A 1 65  ? -7.000  -1.376  8.693   1.00 13.02  ? 65  SER A N   1 
ATOM   551  C  CA  . SER A 1 65  ? -5.649  -1.864  8.703   1.00 10.91  ? 65  SER A CA  1 
ATOM   552  C  C   . SER A 1 65  ? -4.950  -1.110  9.840   1.00 11.23  ? 65  SER A C   1 
ATOM   553  O  O   . SER A 1 65  ? -5.635  -0.448  10.617  1.00 14.41  ? 65  SER A O   1 
ATOM   554  C  CB  . SER A 1 65  ? -4.991  -1.661  7.347   1.00 11.89  ? 65  SER A CB  1 
ATOM   555  O  OG  . SER A 1 65  ? -3.731  -2.276  7.418   1.00 13.87  ? 65  SER A OG  1 
ATOM   556  N  N   . PHE A 1 66  ? -3.627  -1.216  9.950   1.00 11.87  ? 66  PHE A N   1 
ATOM   557  C  CA  . PHE A 1 66  ? -2.831  -0.276  10.718  1.00 13.61  ? 66  PHE A CA  1 
ATOM   558  C  C   . PHE A 1 66  ? -1.984  0.582   9.781   1.00 13.02  ? 66  PHE A C   1 
ATOM   559  O  O   . PHE A 1 66  ? -1.628  0.140   8.687   1.00 11.83  ? 66  PHE A O   1 
ATOM   560  C  CB  . PHE A 1 66  ? -1.975  -1.030  11.769  1.00 13.09  ? 66  PHE A CB  1 
ATOM   561  C  CG  . PHE A 1 66  ? -0.867  -1.872  11.196  1.00 13.54  ? 66  PHE A CG  1 
ATOM   562  C  CD1 . PHE A 1 66  ? 0.380   -1.283  10.958  1.00 14.52  ? 66  PHE A CD1 1 
ATOM   563  C  CD2 . PHE A 1 66  ? -1.081  -3.224  10.842  1.00 10.98  ? 66  PHE A CD2 1 
ATOM   564  C  CE1 . PHE A 1 66  ? 1.415   -2.035  10.416  1.00 15.71  ? 66  PHE A CE1 1 
ATOM   565  C  CE2 . PHE A 1 66  ? 0.012   -3.961  10.371  1.00 14.98  ? 66  PHE A CE2 1 
ATOM   566  C  CZ  . PHE A 1 66  ? 1.248   -3.374  10.120  1.00 15.31  ? 66  PHE A CZ  1 
ATOM   567  N  N   A GLN A 1 67  ? -1.324  1.705   10.229  0.50 10.30  ? 67  GLN A N   1 
ATOM   568  N  N   B GLN A 1 67  ? -2.044  1.825   10.198  0.50 12.34  ? 67  GLN A N   1 
ATOM   569  C  CA  A GLN A 1 67  ? -0.512  2.664   9.435   0.50 9.14   ? 67  GLN A CA  1 
ATOM   570  C  CA  B GLN A 1 67  ? -1.416  2.814   9.390   0.50 11.28  ? 67  GLN A CA  1 
ATOM   571  C  C   A GLN A 1 67  ? 0.647   3.330   10.181  0.50 7.31   ? 67  GLN A C   1 
ATOM   572  C  C   B GLN A 1 67  ? -0.372  3.382   10.325  0.50 11.39  ? 67  GLN A C   1 
ATOM   573  O  O   A GLN A 1 67  ? 0.408   3.822   11.283  0.50 9.46   ? 67  GLN A O   1 
ATOM   574  O  O   B GLN A 1 67  ? -0.614  3.755   11.483  0.50 11.59  ? 67  GLN A O   1 
ATOM   575  C  CB  A GLN A 1 67  ? -1.346  3.756   8.737   0.50 8.84   ? 67  GLN A CB  1 
ATOM   576  C  CB  B GLN A 1 67  ? -2.366  3.899   8.863   0.50 9.69   ? 67  GLN A CB  1 
ATOM   577  C  CG  A GLN A 1 67  ? -2.183  4.618   9.712   0.50 9.89   ? 67  GLN A CG  1 
ATOM   578  C  CG  B GLN A 1 67  ? -3.206  4.550   9.973   0.50 8.79   ? 67  GLN A CG  1 
ATOM   579  C  CD  A GLN A 1 67  ? -3.151  5.545   9.016   0.50 11.90  ? 67  GLN A CD  1 
ATOM   580  C  CD  B GLN A 1 67  ? -4.258  5.530   9.468   0.50 11.37  ? 67  GLN A CD  1 
ATOM   581  O  OE1 A GLN A 1 67  ? -3.965  5.078   8.211   0.50 14.39  ? 67  GLN A OE1 1 
ATOM   582  O  OE1 B GLN A 1 67  ? -4.345  6.732   9.840   0.50 12.96  ? 67  GLN A OE1 1 
ATOM   583  N  NE2 A GLN A 1 67  ? -3.152  6.815   9.384   0.50 13.02  ? 67  GLN A NE2 1 
ATOM   584  N  NE2 B GLN A 1 67  ? -5.130  5.010   8.638   0.50 11.99  ? 67  GLN A NE2 1 
ATOM   585  N  N   A VAL A 1 68  ? 1.851   3.293   9.609   0.50 9.23   ? 68  VAL A N   1 
ATOM   586  N  N   B VAL A 1 68  ? 0.841   3.476   9.786   0.50 9.99   ? 68  VAL A N   1 
ATOM   587  C  CA  A VAL A 1 68  ? 3.012   4.015   10.122  0.50 8.54   ? 68  VAL A CA  1 
ATOM   588  C  CA  B VAL A 1 68  ? 1.895   4.270   10.401  0.50 11.23  ? 68  VAL A CA  1 
ATOM   589  C  C   A VAL A 1 68  ? 3.086   5.369   9.429   0.50 9.51   ? 68  VAL A C   1 
ATOM   590  C  C   B VAL A 1 68  ? 1.882   5.564   9.589   0.50 8.65   ? 68  VAL A C   1 
ATOM   591  O  O   A VAL A 1 68  ? 3.125   5.434   8.214   0.50 10.14  ? 68  VAL A O   1 
ATOM   592  O  O   B VAL A 1 68  ? 2.098   5.508   8.384   0.50 10.46  ? 68  VAL A O   1 
ATOM   593  C  CB  A VAL A 1 68  ? 4.355   3.271   9.996   0.50 9.14   ? 68  VAL A CB  1 
ATOM   594  C  CB  B VAL A 1 68  ? 3.230   3.502   10.286  0.50 11.79  ? 68  VAL A CB  1 
ATOM   595  C  CG1 A VAL A 1 68  ? 5.518   4.159   10.409  0.50 9.75   ? 68  VAL A CG1 1 
ATOM   596  C  CG1 B VAL A 1 68  ? 4.380   4.330   10.834  0.50 12.78  ? 68  VAL A CG1 1 
ATOM   597  C  CG2 A VAL A 1 68  ? 4.361   1.979   10.806  0.50 8.06   ? 68  VAL A CG2 1 
ATOM   598  C  CG2 B VAL A 1 68  ? 3.211   2.117   10.979  0.50 13.78  ? 68  VAL A CG2 1 
ATOM   599  N  N   A GLU A 1 69  ? 2.808   6.420   10.212  0.50 8.86   ? 69  GLU A N   1 
ATOM   600  N  N   B GLU A 1 69  ? 1.915   6.684   10.286  0.50 7.72   ? 69  GLU A N   1 
ATOM   601  C  CA  A GLU A 1 69  ? 2.722   7.781   9.726   0.50 7.56   ? 69  GLU A CA  1 
ATOM   602  C  CA  B GLU A 1 69  ? 1.949   8.002   9.673   0.50 8.94   ? 69  GLU A CA  1 
ATOM   603  C  C   A GLU A 1 69  ? 4.011   8.437   9.772   0.50 7.49   ? 69  GLU A C   1 
ATOM   604  C  C   B GLU A 1 69  ? 3.350   8.712   9.947   0.50 9.93   ? 69  GLU A C   1 
ATOM   605  O  O   A GLU A 1 69  ? 4.787   8.354   10.744  0.50 7.32   ? 69  GLU A O   1 
ATOM   606  O  O   B GLU A 1 69  ? 3.805   8.547   11.077  0.50 8.91   ? 69  GLU A O   1 
ATOM   607  C  CB  A GLU A 1 69  ? 1.763   8.593   10.549  0.50 8.80   ? 69  GLU A CB  1 
ATOM   608  C  CB  B GLU A 1 69  ? 0.665   8.710   10.182  0.50 9.78   ? 69  GLU A CB  1 
ATOM   609  C  CG  A GLU A 1 69  ? 0.323   8.310   10.265  0.50 8.43   ? 69  GLU A CG  1 
ATOM   610  C  CG  B GLU A 1 69  ? -0.674  8.002   9.895   0.50 10.51  ? 69  GLU A CG  1 
ATOM   611  C  CD  A GLU A 1 69  ? -0.596  8.531   11.473  0.50 7.80   ? 69  GLU A CD  1 
ATOM   612  C  CD  B GLU A 1 69  ? -1.887  8.864   10.204  0.50 11.92  ? 69  GLU A CD  1 
ATOM   613  O  OE1 A GLU A 1 69  ? -0.149  9.183   12.447  0.50 8.90   ? 69  GLU A OE1 1 
ATOM   614  O  OE1 B GLU A 1 69  ? -2.500  8.584   11.253  0.50 12.91  ? 69  GLU A OE1 1 
ATOM   615  O  OE2 A GLU A 1 69  ? -1.780  8.112   11.435  0.50 9.95   ? 69  GLU A OE2 1 
ATOM   616  O  OE2 B GLU A 1 69  ? -2.199  9.784   9.401   0.50 13.03  ? 69  GLU A OE2 1 
ATOM   617  N  N   . PHE A 1 70  ? 3.989   9.431   8.951   1.00 14.62  ? 70  PHE A N   1 
ATOM   618  C  CA  . PHE A 1 70  ? 5.253   10.191  8.875   1.00 16.71  ? 70  PHE A CA  1 
ATOM   619  C  C   . PHE A 1 70  ? 5.012   11.695  8.936   1.00 18.05  ? 70  PHE A C   1 
ATOM   620  O  O   . PHE A 1 70  ? 3.977   12.200  8.558   1.00 16.08  ? 70  PHE A O   1 
ATOM   621  C  CB  . PHE A 1 70  ? 6.021   9.830   7.590   1.00 14.47  ? 70  PHE A CB  1 
ATOM   622  C  CG  . PHE A 1 70  ? 6.566   8.416   7.602   1.00 14.98  ? 70  PHE A CG  1 
ATOM   623  C  CD1 . PHE A 1 70  ? 5.731   7.318   7.336   1.00 15.87  ? 70  PHE A CD1 1 
ATOM   624  C  CD2 . PHE A 1 70  ? 7.898   8.198   7.919   1.00 15.14  ? 70  PHE A CD2 1 
ATOM   625  C  CE1 . PHE A 1 70  ? 6.264   6.034   7.420   1.00 15.99  ? 70  PHE A CE1 1 
ATOM   626  C  CE2 . PHE A 1 70  ? 8.413   6.910   7.956   1.00 15.74  ? 70  PHE A CE2 1 
ATOM   627  C  CZ  . PHE A 1 70  ? 7.578   5.818   7.766   1.00 15.49  ? 70  PHE A CZ  1 
ATOM   628  N  N   . ASP A 1 71  ? 6.036   12.427  9.352   1.00 21.07  ? 71  ASP A N   1 
ATOM   629  C  CA  . ASP A 1 71  ? 5.990   13.864  9.212   1.00 18.51  ? 71  ASP A CA  1 
ATOM   630  C  C   . ASP A 1 71  ? 6.146   14.234  7.741   1.00 18.18  ? 71  ASP A C   1 
ATOM   631  O  O   . ASP A 1 71  ? 7.187   13.986  7.184   1.00 24.13  ? 71  ASP A O   1 
ATOM   632  C  CB  . ASP A 1 71  ? 7.138   14.429  10.058  1.00 18.80  ? 71  ASP A CB  1 
ATOM   633  C  CG  . ASP A 1 71  ? 7.305   15.941  9.840   1.00 24.29  ? 71  ASP A CG  1 
ATOM   634  O  OD1 . ASP A 1 71  ? 6.421   16.547  9.287   1.00 19.88  ? 71  ASP A OD1 1 
ATOM   635  O  OD2 . ASP A 1 71  ? 8.346   16.513  10.167  1.00 28.56  ? 71  ASP A OD2 1 
ATOM   636  N  N   . ASP A 1 72  ? 5.107   14.783  7.110   1.00 16.51  ? 72  ASP A N   1 
ATOM   637  C  CA  . ASP A 1 72  ? 5.153   15.158  5.706   1.00 17.50  ? 72  ASP A CA  1 
ATOM   638  C  C   . ASP A 1 72  ? 5.020   16.685  5.607   1.00 18.20  ? 72  ASP A C   1 
ATOM   639  O  O   . ASP A 1 72  ? 4.457   17.174  4.620   1.00 20.29  ? 72  ASP A O   1 
ATOM   640  C  CB  . ASP A 1 72  ? 3.982   14.509  4.920   1.00 15.77  ? 72  ASP A CB  1 
ATOM   641  C  CG  . ASP A 1 72  ? 2.587   14.910  5.422   1.00 17.74  ? 72  ASP A CG  1 
ATOM   642  O  OD1 . ASP A 1 72  ? 2.459   15.509  6.510   1.00 20.96  ? 72  ASP A OD1 1 
ATOM   643  O  OD2 . ASP A 1 72  ? 1.611   14.589  4.718   1.00 18.72  ? 72  ASP A OD2 1 
ATOM   644  N  N   . SER A 1 73  ? 5.523   17.406  6.609   1.00 17.14  ? 73  SER A N   1 
ATOM   645  C  CA  . SER A 1 73  ? 5.454   18.869  6.563   1.00 19.98  ? 73  SER A CA  1 
ATOM   646  C  C   . SER A 1 73  ? 6.666   19.498  5.861   1.00 21.90  ? 73  SER A C   1 
ATOM   647  O  O   . SER A 1 73  ? 6.711   20.714  5.744   1.00 23.64  ? 73  SER A O   1 
ATOM   648  C  CB  . SER A 1 73  ? 5.285   19.496  7.943   1.00 21.17  ? 73  SER A CB  1 
ATOM   649  O  OG  . SER A 1 73  ? 6.445   19.275  8.716   1.00 18.71  ? 73  SER A OG  1 
ATOM   650  N  N   . GLN A 1 74  ? 7.651   18.684  5.412   1.00 19.50  ? 74  GLN A N   1 
ATOM   651  C  CA  . GLN A 1 74  ? 8.845   19.122  4.667   1.00 24.46  ? 74  GLN A CA  1 
ATOM   652  C  C   . GLN A 1 74  ? 9.245   17.934  3.796   1.00 21.54  ? 74  GLN A C   1 
ATOM   653  O  O   . GLN A 1 74  ? 8.747   16.833  4.068   1.00 18.60  ? 74  GLN A O   1 
ATOM   654  C  CB  . GLN A 1 74  ? 10.041  19.275  5.620   1.00 32.89  ? 74  GLN A CB  1 
ATOM   655  C  CG  . GLN A 1 74  ? 10.054  20.438  6.579   1.00 38.48  ? 74  GLN A CG  1 
ATOM   656  C  CD  . GLN A 1 74  ? 11.402  20.406  7.257   1.00 36.04  ? 74  GLN A CD  1 
ATOM   657  O  OE1 . GLN A 1 74  ? 12.451  20.674  6.638   1.00 51.64  ? 74  GLN A OE1 1 
ATOM   658  N  NE2 . GLN A 1 74  ? 11.401  20.025  8.534   1.00 31.99  ? 74  GLN A NE2 1 
ATOM   659  N  N   . ASP A 1 75  ? 10.067  18.154  2.737   1.00 23.16  ? 75  ASP A N   1 
ATOM   660  C  CA  . ASP A 1 75  ? 10.588  17.096  1.841   1.00 22.03  ? 75  ASP A CA  1 
ATOM   661  C  C   . ASP A 1 75  ? 11.670  16.292  2.578   1.00 28.76  ? 75  ASP A C   1 
ATOM   662  O  O   . ASP A 1 75  ? 12.846  16.633  2.505   1.00 46.89  ? 75  ASP A O   1 
ATOM   663  C  CB  . ASP A 1 75  ? 11.186  17.675  0.540   1.00 24.49  ? 75  ASP A CB  1 
ATOM   664  C  CG  . ASP A 1 75  ? 10.183  18.235  -0.475  1.00 25.98  ? 75  ASP A CG  1 
ATOM   665  O  OD1 . ASP A 1 75  ? 8.943   18.115  -0.244  1.00 25.71  ? 75  ASP A OD1 1 
ATOM   666  O  OD2 . ASP A 1 75  ? 10.654  18.764  -1.515  1.00 39.43  ? 75  ASP A OD2 1 
ATOM   667  N  N   . LYS A 1 76  ? 11.272  15.322  3.378   1.00 21.14  ? 76  LYS A N   1 
ATOM   668  C  CA  . LYS A 1 76  ? 12.202  14.438  4.021   1.00 19.53  ? 76  LYS A CA  1 
ATOM   669  C  C   . LYS A 1 76  ? 12.190  13.160  3.174   1.00 29.55  ? 76  LYS A C   1 
ATOM   670  O  O   . LYS A 1 76  ? 12.958  13.033  2.215   1.00 42.90  ? 76  LYS A O   1 
ATOM   671  C  CB  . LYS A 1 76  ? 11.594  14.197  5.405   1.00 26.53  ? 76  LYS A CB  1 
ATOM   672  C  CG  . LYS A 1 76  ? 11.799  15.404  6.313   1.00 23.33  ? 76  LYS A CG  1 
ATOM   673  C  CD  . LYS A 1 76  ? 11.100  15.286  7.662   1.00 29.31  ? 76  LYS A CD  1 
ATOM   674  C  CE  . LYS A 1 76  ? 11.797  16.145  8.699   1.00 23.54  ? 76  LYS A CE  1 
ATOM   675  N  NZ  . LYS A 1 76  ? 11.612  15.659  10.084  1.00 30.19  ? 76  LYS A NZ  1 
ATOM   676  N  N   . ALA A 1 77  ? 11.169  12.303  3.416   1.00 24.90  ? 77  ALA A N   1 
ATOM   677  C  CA  . ALA A 1 77  ? 11.051  10.991  2.786   1.00 17.41  ? 77  ALA A CA  1 
ATOM   678  C  C   . ALA A 1 77  ? 10.285  11.280  1.475   1.00 15.52  ? 77  ALA A C   1 
ATOM   679  O  O   . ALA A 1 77  ? 9.073   11.560  1.552   1.00 15.91  ? 77  ALA A O   1 
ATOM   680  C  CB  . ALA A 1 77  ? 10.194  10.110  3.664   1.00 23.72  ? 77  ALA A CB  1 
ATOM   681  N  N   . VAL A 1 78  ? 10.906  11.110  0.284   1.00 15.01  ? 78  VAL A N   1 
ATOM   682  C  CA  . VAL A 1 78  ? 10.265  11.414  -0.995  1.00 14.56  ? 78  VAL A CA  1 
ATOM   683  C  C   . VAL A 1 78  ? 10.499  10.306  -2.045  1.00 13.02  ? 78  VAL A C   1 
ATOM   684  O  O   . VAL A 1 78  ? 11.539  9.648   -2.049  1.00 15.54  ? 78  VAL A O   1 
ATOM   685  C  CB  . VAL A 1 78  ? 10.605  12.814  -1.528  1.00 17.00  ? 78  VAL A CB  1 
ATOM   686  C  CG1 . VAL A 1 78  ? 10.388  13.899  -0.504  1.00 19.78  ? 78  VAL A CG1 1 
ATOM   687  C  CG2 . VAL A 1 78  ? 12.025  12.880  -1.916  1.00 18.64  ? 78  VAL A CG2 1 
ATOM   688  N  N   . LEU A 1 79  ? 9.518   10.190  -2.968  1.00 11.48  ? 79  LEU A N   1 
ATOM   689  C  CA  . LEU A 1 79  ? 9.612   9.359   -4.141  1.00 10.90  ? 79  LEU A CA  1 
ATOM   690  C  C   . LEU A 1 79  ? 9.608   10.239  -5.353  1.00 11.95  ? 79  LEU A C   1 
ATOM   691  O  O   . LEU A 1 79  ? 8.780   11.145  -5.464  1.00 12.54  ? 79  LEU A O   1 
ATOM   692  C  CB  . LEU A 1 79  ? 8.370   8.437   -4.166  1.00 13.10  ? 79  LEU A CB  1 
ATOM   693  C  CG  . LEU A 1 79  ? 8.227   7.385   -5.234  1.00 12.95  ? 79  LEU A CG  1 
ATOM   694  C  CD1 . LEU A 1 79  ? 9.319   6.352   -4.961  1.00 16.89  ? 79  LEU A CD1 1 
ATOM   695  C  CD2 . LEU A 1 79  ? 6.806   6.701   -5.113  1.00 10.70  ? 79  LEU A CD2 1 
ATOM   696  N  N   . LYS A 1 80  ? 10.535  9.963   -6.269  1.00 12.65  ? 80  LYS A N   1 
ATOM   697  C  CA  . LYS A 1 80  ? 10.559  10.657  -7.555  1.00 14.10  ? 80  LYS A CA  1 
ATOM   698  C  C   . LYS A 1 80  ? 11.042  9.696   -8.645  1.00 12.55  ? 80  LYS A C   1 
ATOM   699  O  O   . LYS A 1 80  ? 11.300  8.542   -8.355  1.00 13.59  ? 80  LYS A O   1 
ATOM   700  C  CB  . LYS A 1 80  ? 11.435  11.911  -7.478  1.00 21.33  ? 80  LYS A CB  1 
ATOM   701  C  CG  . LYS A 1 80  ? 12.513  11.813  -6.412  1.00 36.18  ? 80  LYS A CG  1 
ATOM   702  C  CD  . LYS A 1 80  ? 13.096  13.117  -5.882  1.00 121.85 ? 80  LYS A CD  1 
ATOM   703  C  CE  . LYS A 1 80  ? 14.542  12.954  -5.395  1.00 54.79  ? 80  LYS A CE  1 
ATOM   704  N  NZ  . LYS A 1 80  ? 14.737  13.237  -3.907  1.00 38.75  ? 80  LYS A NZ  1 
ATOM   705  N  N   . GLY A 1 81  ? 11.175  10.214  -9.858  1.00 14.18  ? 81  GLY A N   1 
ATOM   706  C  CA  . GLY A 1 81  ? 11.578  9.444   -11.030 1.00 15.99  ? 81  GLY A CA  1 
ATOM   707  C  C   . GLY A 1 81  ? 10.571  8.342   -11.326 1.00 18.02  ? 81  GLY A C   1 
ATOM   708  O  O   . GLY A 1 81  ? 9.401   8.471   -11.068 1.00 12.94  ? 81  GLY A O   1 
ATOM   709  N  N   . GLY A 1 82  ? 11.086  7.254   -11.862 1.00 22.37  ? 82  GLY A N   1 
ATOM   710  C  CA  . GLY A 1 82  ? 10.179  6.246   -12.368 1.00 21.35  ? 82  GLY A CA  1 
ATOM   711  C  C   . GLY A 1 82  ? 9.234   6.844   -13.409 1.00 17.93  ? 82  GLY A C   1 
ATOM   712  O  O   . GLY A 1 82  ? 9.675   7.581   -14.296 1.00 29.10  ? 82  GLY A O   1 
ATOM   713  N  N   . PRO A 1 83  ? 7.904   6.630   -13.276 1.00 15.52  ? 83  PRO A N   1 
ATOM   714  C  CA  . PRO A 1 83  ? 6.948   7.304   -14.160 1.00 14.79  ? 83  PRO A CA  1 
ATOM   715  C  C   . PRO A 1 83  ? 6.574   8.735   -13.738 1.00 14.10  ? 83  PRO A C   1 
ATOM   716  O  O   . PRO A 1 83  ? 5.768   9.357   -14.428 1.00 19.32  ? 83  PRO A O   1 
ATOM   717  C  CB  . PRO A 1 83  ? 5.698   6.351   -14.013 1.00 13.89  ? 83  PRO A CB  1 
ATOM   718  C  CG  . PRO A 1 83  ? 5.800   5.973   -12.575 1.00 13.01  ? 83  PRO A CG  1 
ATOM   719  C  CD  . PRO A 1 83  ? 7.260   5.728   -12.302 1.00 15.26  ? 83  PRO A CD  1 
ATOM   720  N  N   . LEU A 1 84  ? 7.075   9.182   -12.581 1.00 11.43  ? 84  LEU A N   1 
ATOM   721  C  CA  . LEU A 1 84  ? 6.530   10.372  -11.930 1.00 12.50  ? 84  LEU A CA  1 
ATOM   722  C  C   . LEU A 1 84  ? 7.172   11.607  -12.509 1.00 16.51  ? 84  LEU A C   1 
ATOM   723  O  O   . LEU A 1 84  ? 8.396   11.631  -12.806 1.00 23.56  ? 84  LEU A O   1 
ATOM   724  C  CB  . LEU A 1 84  ? 6.852   10.305  -10.452 1.00 12.08  ? 84  LEU A CB  1 
ATOM   725  C  CG  . LEU A 1 84  ? 6.283   9.045   -9.786  1.00 11.81  ? 84  LEU A CG  1 
ATOM   726  C  CD1 . LEU A 1 84  ? 6.700   8.952   -8.338  1.00 13.93  ? 84  LEU A CD1 1 
ATOM   727  C  CD2 . LEU A 1 84  ? 4.712   9.034   -9.884  1.00 12.02  ? 84  LEU A CD2 1 
ATOM   728  N  N   . ASP A 1 85  ? 6.401   12.692  -12.500 1.00 14.05  ? 85  ASP A N   1 
ATOM   729  C  CA  . ASP A 1 85  ? 6.900   14.040  -12.757 1.00 16.77  ? 85  ASP A CA  1 
ATOM   730  C  C   . ASP A 1 85  ? 6.867   14.720  -11.379 1.00 19.49  ? 85  ASP A C   1 
ATOM   731  O  O   . ASP A 1 85  ? 5.876   14.581  -10.681 1.00 26.41  ? 85  ASP A O   1 
ATOM   732  C  CB  . ASP A 1 85  ? 6.000   14.766  -13.800 1.00 23.91  ? 85  ASP A CB  1 
ATOM   733  C  CG  . ASP A 1 85  ? 6.185   14.322  -15.249 1.00 30.96  ? 85  ASP A CG  1 
ATOM   734  O  OD1 . ASP A 1 85  ? 7.174   13.584  -15.519 1.00 40.74  ? 85  ASP A OD1 1 
ATOM   735  O  OD2 . ASP A 1 85  ? 5.359   14.743  -16.123 1.00 36.35  ? 85  ASP A OD2 1 
ATOM   736  N  N   . GLY A 1 86  ? 7.916   15.413  -10.968 1.00 24.41  ? 86  GLY A N   1 
ATOM   737  C  CA  . GLY A 1 86  ? 7.930   16.023  -9.654  1.00 23.90  ? 86  GLY A CA  1 
ATOM   738  C  C   . GLY A 1 86  ? 8.147   15.071  -8.468  1.00 17.15  ? 86  GLY A C   1 
ATOM   739  O  O   . GLY A 1 86  ? 8.593   13.915  -8.574  1.00 24.17  ? 86  GLY A O   1 
ATOM   740  N  N   . THR A 1 87  ? 7.820   15.593  -7.280  1.00 14.52  ? 87  THR A N   1 
ATOM   741  C  CA  . THR A 1 87  ? 8.249   15.033  -6.005  1.00 14.78  ? 87  THR A CA  1 
ATOM   742  C  C   . THR A 1 87  ? 7.015   14.657  -5.202  1.00 13.35  ? 87  THR A C   1 
ATOM   743  O  O   . THR A 1 87  ? 6.084   15.465  -5.051  1.00 11.70  ? 87  THR A O   1 
ATOM   744  C  CB  . THR A 1 87  ? 8.962   16.158  -5.201  1.00 29.02  ? 87  THR A CB  1 
ATOM   745  O  OG1 . THR A 1 87  ? 10.129  16.680  -5.890  1.00 43.84  ? 87  THR A OG1 1 
ATOM   746  C  CG2 . THR A 1 87  ? 9.551   15.671  -3.880  1.00 32.57  ? 87  THR A CG2 1 
ATOM   747  N  N   . TYR A 1 88  ? 7.097   13.488  -4.589  1.00 11.73  ? 88  TYR A N   1 
ATOM   748  C  CA  . TYR A 1 88  ? 5.924   12.959  -3.852  1.00 11.85  ? 88  TYR A CA  1 
ATOM   749  C  C   . TYR A 1 88  ? 6.398   12.650  -2.427  1.00 11.44  ? 88  TYR A C   1 
ATOM   750  O  O   . TYR A 1 88  ? 7.372   11.896  -2.280  1.00 14.63  ? 88  TYR A O   1 
ATOM   751  C  CB  . TYR A 1 88  ? 5.372   11.694  -4.526  1.00 9.99   ? 88  TYR A CB  1 
ATOM   752  C  CG  . TYR A 1 88  ? 4.624   11.891  -5.812  1.00 9.85   ? 88  TYR A CG  1 
ATOM   753  C  CD1 . TYR A 1 88  ? 5.283   12.273  -6.966  1.00 9.25   ? 88  TYR A CD1 1 
ATOM   754  C  CD2 . TYR A 1 88  ? 3.263   11.655  -5.872  1.00 8.99   ? 88  TYR A CD2 1 
ATOM   755  C  CE1 . TYR A 1 88  ? 4.599   12.438  -8.155  1.00 9.61   ? 88  TYR A CE1 1 
ATOM   756  C  CE2 . TYR A 1 88  ? 2.562   11.815  -7.052  1.00 8.31   ? 88  TYR A CE2 1 
ATOM   757  C  CZ  . TYR A 1 88  ? 3.237   12.207  -8.191  1.00 7.57   ? 88  TYR A CZ  1 
ATOM   758  O  OH  . TYR A 1 88  ? 2.555   12.363  -9.351  1.00 8.83   ? 88  TYR A OH  1 
ATOM   759  N  N   . ARG A 1 89  ? 5.757   13.243  -1.414  1.00 10.46  ? 89  ARG A N   1 
ATOM   760  C  CA  . ARG A 1 89  ? 6.189   13.081  -0.024  1.00 11.49  ? 89  ARG A CA  1 
ATOM   761  C  C   . ARG A 1 89  ? 5.500   11.862  0.621   1.00 10.10  ? 89  ARG A C   1 
ATOM   762  O  O   . ARG A 1 89  ? 4.278   11.689  0.464   1.00 9.54   ? 89  ARG A O   1 
ATOM   763  C  CB  . ARG A 1 89  ? 5.689   14.304  0.764   1.00 15.44  ? 89  ARG A CB  1 
ATOM   764  C  CG  . ARG A 1 89  ? 6.604   15.511  0.861   1.00 18.84  ? 89  ARG A CG  1 
ATOM   765  C  CD  . ARG A 1 89  ? 6.128   16.529  1.869   1.00 22.48  ? 89  ARG A CD  1 
ATOM   766  N  NE  . ARG A 1 89  ? 6.687   17.863  1.521   1.00 21.77  ? 89  ARG A NE  1 
ATOM   767  C  CZ  . ARG A 1 89  ? 6.214   19.056  1.913   1.00 19.49  ? 89  ARG A CZ  1 
ATOM   768  N  NH1 . ARG A 1 89  ? 5.138   19.155  2.689   1.00 19.93  ? 89  ARG A NH1 1 
ATOM   769  N  NH2 . ARG A 1 89  ? 6.752   20.161  1.426   1.00 33.16  ? 89  ARG A NH2 1 
ATOM   770  N  N   . LEU A 1 90  ? 6.310   11.059  1.337   1.00 9.64   ? 90  LEU A N   1 
ATOM   771  C  CA  . LEU A 1 90  ? 5.730   9.905   2.047   1.00 10.94  ? 90  LEU A CA  1 
ATOM   772  C  C   . LEU A 1 90  ? 4.837   10.377  3.186   1.00 9.82   ? 90  LEU A C   1 
ATOM   773  O  O   . LEU A 1 90  ? 5.343   11.155  4.052   1.00 13.48  ? 90  LEU A O   1 
ATOM   774  C  CB  . LEU A 1 90  ? 6.869   9.065   2.622   1.00 12.63  ? 90  LEU A CB  1 
ATOM   775  C  CG  . LEU A 1 90  ? 6.432   7.874   3.481   1.00 13.21  ? 90  LEU A CG  1 
ATOM   776  C  CD1 . LEU A 1 90  ? 5.652   6.839   2.635   1.00 14.56  ? 90  LEU A CD1 1 
ATOM   777  C  CD2 . LEU A 1 90  ? 7.624   7.172   4.088   1.00 16.07  ? 90  LEU A CD2 1 
ATOM   778  N  N   . LEU A 1 91  ? 3.598   9.949   3.227   1.00 9.82   ? 91  LEU A N   1 
ATOM   779  C  CA  . LEU A 1 91  ? 2.642   10.211  4.294   1.00 10.42  ? 91  LEU A CA  1 
ATOM   780  C  C   . LEU A 1 91  ? 2.500   9.072   5.249   1.00 9.98   ? 91  LEU A C   1 
ATOM   781  O  O   . LEU A 1 91  ? 2.480   9.319   6.447   1.00 10.94  ? 91  LEU A O   1 
ATOM   782  C  CB  . LEU A 1 91  ? 1.312   10.568  3.601   1.00 13.10  ? 91  LEU A CB  1 
ATOM   783  C  CG  . LEU A 1 91  ? 0.093   10.685  4.522   1.00 12.45  ? 91  LEU A CG  1 
ATOM   784  C  CD1 . LEU A 1 91  ? 0.326   11.790  5.567   1.00 20.57  ? 91  LEU A CD1 1 
ATOM   785  C  CD2 . LEU A 1 91  ? -1.118  11.052  3.758   1.00 18.25  ? 91  LEU A CD2 1 
ATOM   786  N  N   A GLN A 1 92  ? 2.291   7.852   4.743   0.50 11.02  ? 92  GLN A N   1 
ATOM   787  N  N   B GLN A 1 92  ? 2.300   7.852   4.732   0.50 10.85  ? 92  GLN A N   1 
ATOM   788  C  CA  A GLN A 1 92  ? 2.045   6.751   5.648   0.50 12.60  ? 92  GLN A CA  1 
ATOM   789  C  CA  B GLN A 1 92  ? 1.970   6.718   5.573   0.50 11.77  ? 92  GLN A CA  1 
ATOM   790  C  C   A GLN A 1 92  ? 2.183   5.456   4.857   0.50 9.78   ? 92  GLN A C   1 
ATOM   791  C  C   B GLN A 1 92  ? 2.386   5.456   4.823   0.50 10.17  ? 92  GLN A C   1 
ATOM   792  O  O   A GLN A 1 92  ? 2.087   5.464   3.625   0.50 8.07   ? 92  GLN A O   1 
ATOM   793  O  O   B GLN A 1 92  ? 2.659   5.478   3.620   0.50 7.81   ? 92  GLN A O   1 
ATOM   794  C  CB  A GLN A 1 92  ? 0.631   6.860   6.209   0.50 12.97  ? 92  GLN A CB  1 
ATOM   795  C  CB  B GLN A 1 92  ? 0.499   6.664   6.056   0.50 11.11  ? 92  GLN A CB  1 
ATOM   796  C  CG  A GLN A 1 92  ? -0.386  6.852   5.075   0.50 11.94  ? 92  GLN A CG  1 
ATOM   797  C  CG  B GLN A 1 92  ? -0.584  6.470   4.982   0.50 10.85  ? 92  GLN A CG  1 
ATOM   798  C  CD  A GLN A 1 92  ? -1.156  5.531   5.075   0.50 8.32   ? 92  GLN A CD  1 
ATOM   799  C  CD  B GLN A 1 92  ? -1.842  5.801   5.529   0.50 11.23  ? 92  GLN A CD  1 
ATOM   800  O  OE1 A GLN A 1 92  ? -0.689  4.463   4.772   0.50 8.57   ? 92  GLN A OE1 1 
ATOM   801  O  OE1 B GLN A 1 92  ? -2.726  6.400   6.170   0.50 13.43  ? 92  GLN A OE1 1 
ATOM   802  N  NE2 A GLN A 1 92  ? -2.424  5.596   5.405   0.50 12.01  ? 92  GLN A NE2 1 
ATOM   803  N  NE2 B GLN A 1 92  ? -1.963  4.519   5.262   0.50 12.59  ? 92  GLN A NE2 1 
ATOM   804  N  N   . PHE A 1 93  ? 2.483   4.368   5.579   1.00 10.87  ? 93  PHE A N   1 
ATOM   805  C  CA  . PHE A 1 93  ? 2.343   3.059   4.976   1.00 10.03  ? 93  PHE A CA  1 
ATOM   806  C  C   . PHE A 1 93  ? 1.372   2.224   5.772   1.00 9.62   ? 93  PHE A C   1 
ATOM   807  O  O   . PHE A 1 93  ? 1.101   2.435   6.957   1.00 12.03  ? 93  PHE A O   1 
ATOM   808  C  CB  . PHE A 1 93  ? 3.655   2.303   4.773   1.00 11.28  ? 93  PHE A CB  1 
ATOM   809  C  CG  . PHE A 1 93  ? 4.426   1.916   6.026   1.00 11.64  ? 93  PHE A CG  1 
ATOM   810  C  CD1 . PHE A 1 93  ? 4.034   0.797   6.762   1.00 12.79  ? 93  PHE A CD1 1 
ATOM   811  C  CD2 . PHE A 1 93  ? 5.565   2.592   6.423   1.00 14.35  ? 93  PHE A CD2 1 
ATOM   812  C  CE1 . PHE A 1 93  ? 4.773   0.396   7.879   1.00 12.36  ? 93  PHE A CE1 1 
ATOM   813  C  CE2 . PHE A 1 93  ? 6.264   2.173   7.538   1.00 15.18  ? 93  PHE A CE2 1 
ATOM   814  C  CZ  . PHE A 1 93  ? 5.885   1.111   8.297   1.00 14.84  ? 93  PHE A CZ  1 
ATOM   815  N  N   . HIS A 1 94  ? 0.798   1.225   5.083   1.00 9.78   ? 94  HIS A N   1 
ATOM   816  C  CA  . HIS A 1 94  ? -0.055  0.257   5.735   1.00 8.42   ? 94  HIS A CA  1 
ATOM   817  C  C   . HIS A 1 94  ? 0.019   -1.022  4.911   1.00 6.40   ? 94  HIS A C   1 
ATOM   818  O  O   . HIS A 1 94  ? 0.653   -1.043  3.891   1.00 7.49   ? 94  HIS A O   1 
ATOM   819  C  CB  . HIS A 1 94  ? -1.515  0.791   5.700   1.00 8.66   ? 94  HIS A CB  1 
ATOM   820  C  CG  . HIS A 1 94  ? -2.080  1.062   4.327   1.00 8.13   ? 94  HIS A CG  1 
ATOM   821  N  ND1 . HIS A 1 94  ? -1.927  2.260   3.685   1.00 7.96   ? 94  HIS A ND1 1 
ATOM   822  C  CD2 . HIS A 1 94  ? -2.606  0.238   3.396   1.00 6.75   ? 94  HIS A CD2 1 
ATOM   823  C  CE1 . HIS A 1 94  ? -2.390  2.157   2.436   1.00 7.03   ? 94  HIS A CE1 1 
ATOM   824  N  NE2 . HIS A 1 94  ? -2.810  0.890   2.225   1.00 5.53   ? 94  HIS A NE2 1 
ATOM   825  N  N   . PHE A 1 95  ? -0.741  -2.012  5.377   1.00 7.31   ? 95  PHE A N   1 
ATOM   826  C  CA  . PHE A 1 95  ? -0.727  -3.346  4.723   1.00 6.49   ? 95  PHE A CA  1 
ATOM   827  C  C   . PHE A 1 95  ? -2.152  -3.845  4.497   1.00 5.58   ? 95  PHE A C   1 
ATOM   828  O  O   . PHE A 1 95  ? -3.081  -3.420  5.110   1.00 7.31   ? 95  PHE A O   1 
ATOM   829  C  CB  . PHE A 1 95  ? 0.001   -4.404  5.582   1.00 7.67   ? 95  PHE A CB  1 
ATOM   830  C  CG  . PHE A 1 95  ? 1.463   -4.139  5.860   1.00 7.00   ? 95  PHE A CG  1 
ATOM   831  C  CD1 . PHE A 1 95  ? 1.836   -3.244  6.828   1.00 8.17   ? 95  PHE A CD1 1 
ATOM   832  C  CD2 . PHE A 1 95  ? 2.462   -4.816  5.166   1.00 7.69   ? 95  PHE A CD2 1 
ATOM   833  C  CE1 . PHE A 1 95  ? 3.148   -3.092  7.151   1.00 9.71   ? 95  PHE A CE1 1 
ATOM   834  C  CE2 . PHE A 1 95  ? 3.810   -4.622  5.437   1.00 9.47   ? 95  PHE A CE2 1 
ATOM   835  C  CZ  . PHE A 1 95  ? 4.195   -3.710  6.445   1.00 9.68   ? 95  PHE A CZ  1 
ATOM   836  N  N   . HIS A 1 96  ? -2.244  -4.797  3.566   1.00 6.78   ? 96  HIS A N   1 
ATOM   837  C  CA  . HIS A 1 96  ? -3.394  -5.604  3.314   1.00 6.22   ? 96  HIS A CA  1 
ATOM   838  C  C   . HIS A 1 96  ? -2.974  -7.047  3.421   1.00 5.89   ? 96  HIS A C   1 
ATOM   839  O  O   . HIS A 1 96  ? -1.887  -7.407  2.993   1.00 6.27   ? 96  HIS A O   1 
ATOM   840  C  CB  . HIS A 1 96  ? -4.013  -5.313  1.937   1.00 6.43   ? 96  HIS A CB  1 
ATOM   841  C  CG  . HIS A 1 96  ? -4.310  -3.895  1.640   1.00 5.81   ? 96  HIS A CG  1 
ATOM   842  N  ND1 . HIS A 1 96  ? -5.570  -3.383  1.823   1.00 5.90   ? 96  HIS A ND1 1 
ATOM   843  C  CD2 . HIS A 1 96  ? -3.511  -2.895  1.269   1.00 6.07   ? 96  HIS A CD2 1 
ATOM   844  C  CE1 . HIS A 1 96  ? -5.506  -2.078  1.539   1.00 5.89   ? 96  HIS A CE1 1 
ATOM   845  N  NE2 . HIS A 1 96  ? -4.258  -1.743  1.202   1.00 5.46   ? 96  HIS A NE2 1 
ATOM   846  N  N   . TRP A 1 97  ? -3.754  -7.895  4.100   1.00 6.08   ? 97  TRP A N   1 
ATOM   847  C  CA  . TRP A 1 97  ? -3.340  -9.273  4.250   1.00 6.48   ? 97  TRP A CA  1 
ATOM   848  C  C   . TRP A 1 97  ? -4.568  -10.176 4.394   1.00 5.64   ? 97  TRP A C   1 
ATOM   849  O  O   . TRP A 1 97  ? -5.720  -9.741  4.495   1.00 6.59   ? 97  TRP A O   1 
ATOM   850  C  CB  . TRP A 1 97  ? -2.475  -9.476  5.517   1.00 6.92   ? 97  TRP A CB  1 
ATOM   851  C  CG  . TRP A 1 97  ? -3.122  -9.102  6.841   1.00 7.02   ? 97  TRP A CG  1 
ATOM   852  C  CD1 . TRP A 1 97  ? -3.821  -9.933  7.643   1.00 8.75   ? 97  TRP A CD1 1 
ATOM   853  C  CD2 . TRP A 1 97  ? -3.197  -7.793  7.440   1.00 7.39   ? 97  TRP A CD2 1 
ATOM   854  N  NE1 . TRP A 1 97  ? -4.296  -9.234  8.726   1.00 9.69   ? 97  TRP A NE1 1 
ATOM   855  C  CE2 . TRP A 1 97  ? -3.868  -7.935  8.636   1.00 8.37   ? 97  TRP A CE2 1 
ATOM   856  C  CE3 . TRP A 1 97  ? -2.626  -6.555  7.132   1.00 8.04   ? 97  TRP A CE3 1 
ATOM   857  C  CZ2 . TRP A 1 97  ? -4.075  -6.838  9.505   1.00 9.60   ? 97  TRP A CZ2 1 
ATOM   858  C  CZ3 . TRP A 1 97  ? -2.837  -5.476  7.974   1.00 9.15   ? 97  TRP A CZ3 1 
ATOM   859  C  CH2 . TRP A 1 97  ? -3.564  -5.619  9.148   1.00 10.09  ? 97  TRP A CH2 1 
ATOM   860  N  N   . GLY A 1 98  ? -4.310  -11.485 4.368   1.00 7.23   ? 98  GLY A N   1 
ATOM   861  C  CA  . GLY A 1 98  ? -5.305  -12.489 4.285   1.00 7.44   ? 98  GLY A CA  1 
ATOM   862  C  C   . GLY A 1 98  ? -5.525  -13.231 5.583   1.00 7.89   ? 98  GLY A C   1 
ATOM   863  O  O   . GLY A 1 98  ? -4.814  -13.098 6.546   1.00 8.20   ? 98  GLY A O   1 
ATOM   864  N  N   . SER A 1 99  ? -6.537  -14.102 5.597   1.00 8.14   ? 99  SER A N   1 
ATOM   865  C  CA  . SER A 1 99  ? -6.736  -15.049 6.665   1.00 8.98   ? 99  SER A CA  1 
ATOM   866  C  C   . SER A 1 99  ? -5.837  -16.281 6.511   1.00 8.60   ? 99  SER A C   1 
ATOM   867  O  O   . SER A 1 99  ? -5.648  -16.991 7.487   1.00 11.66  ? 99  SER A O   1 
ATOM   868  C  CB  . SER A 1 99  ? -8.207  -15.458 6.710   1.00 9.92   ? 99  SER A CB  1 
ATOM   869  O  OG  . SER A 1 99  ? -8.686  -15.893 5.454   1.00 10.09  ? 99  SER A OG  1 
ATOM   870  N  N   . LEU A 1 100 ? -5.363  -16.526 5.287   1.00 8.10   ? 100 LEU A N   1 
ATOM   871  C  CA  . LEU A 1 100 ? -4.488  -17.648 4.952   1.00 10.00  ? 100 LEU A CA  1 
ATOM   872  C  C   . LEU A 1 100 ? -3.407  -17.134 4.048   1.00 8.22   ? 100 LEU A C   1 
ATOM   873  O  O   . LEU A 1 100 ? -3.592  -16.086 3.417   1.00 10.12  ? 100 LEU A O   1 
ATOM   874  C  CB  . LEU A 1 100 ? -5.303  -18.721 4.189   1.00 15.71  ? 100 LEU A CB  1 
ATOM   875  C  CG  . LEU A 1 100 ? -6.608  -19.154 4.831   1.00 17.19  ? 100 LEU A CG  1 
ATOM   876  C  CD1 . LEU A 1 100 ? -7.451  -19.792 3.736   1.00 22.14  ? 100 LEU A CD1 1 
ATOM   877  C  CD2 . LEU A 1 100 ? -6.192  -20.139 5.892   1.00 19.67  ? 100 LEU A CD2 1 
ATOM   878  N  N   . ASP A 1 101 ? -2.313  -17.871 3.958   1.00 7.83   ? 101 ASP A N   1 
ATOM   879  C  CA  . ASP A 1 101 ? -1.177  -17.375 3.221   1.00 8.69   ? 101 ASP A CA  1 
ATOM   880  C  C   . ASP A 1 101 ? -1.418  -17.251 1.713   1.00 8.27   ? 101 ASP A C   1 
ATOM   881  O  O   . ASP A 1 101 ? -0.699  -16.473 1.053   1.00 11.15  ? 101 ASP A O   1 
ATOM   882  C  CB  . ASP A 1 101 ? 0.009   -18.282 3.428   1.00 10.30  ? 101 ASP A CB  1 
ATOM   883  C  CG  . ASP A 1 101 ? 0.535   -18.322 4.835   1.00 12.25  ? 101 ASP A CG  1 
ATOM   884  O  OD1 . ASP A 1 101 ? 0.144   -17.506 5.683   1.00 11.67  ? 101 ASP A OD1 1 
ATOM   885  O  OD2 . ASP A 1 101 ? 1.414   -19.161 5.057   1.00 17.89  ? 101 ASP A OD2 1 
ATOM   886  N  N   . GLY A 1 102 ? -2.434  -17.938 1.164   1.00 8.91   ? 102 GLY A N   1 
ATOM   887  C  CA  . GLY A 1 102 ? -2.705  -17.844 -0.253  1.00 10.37  ? 102 GLY A CA  1 
ATOM   888  C  C   . GLY A 1 102 ? -3.622  -16.714 -0.728  1.00 8.17   ? 102 GLY A C   1 
ATOM   889  O  O   . GLY A 1 102 ? -4.019  -16.684 -1.902  1.00 9.53   ? 102 GLY A O   1 
ATOM   890  N  N   A GLN A 1 103 ? -3.898  -15.776 0.184   0.50 7.93   ? 103 GLN A N   1 
ATOM   891  N  N   B GLN A 1 103 ? -3.882  -15.728 0.118   0.50 9.24   ? 103 GLN A N   1 
ATOM   892  C  CA  A GLN A 1 103 ? -4.640  -14.581 -0.158  0.50 6.52   ? 103 GLN A CA  1 
ATOM   893  C  CA  B GLN A 1 103 ? -4.519  -14.525 -0.373  0.50 8.99   ? 103 GLN A CA  1 
ATOM   894  C  C   A GLN A 1 103 ? -4.243  -13.417 0.724   0.50 5.81   ? 103 GLN A C   1 
ATOM   895  C  C   B GLN A 1 103 ? -4.110  -13.422 0.575   0.50 7.07   ? 103 GLN A C   1 
ATOM   896  O  O   A GLN A 1 103 ? -3.818  -13.639 1.850   0.50 5.51   ? 103 GLN A O   1 
ATOM   897  O  O   B GLN A 1 103 ? -3.495  -13.705 1.599   0.50 7.50   ? 103 GLN A O   1 
ATOM   898  C  CB  A GLN A 1 103 ? -6.124  -14.885 0.011   0.50 7.45   ? 103 GLN A CB  1 
ATOM   899  C  CB  B GLN A 1 103 ? -6.045  -14.731 -0.417  0.50 8.91   ? 103 GLN A CB  1 
ATOM   900  C  CG  A GLN A 1 103 ? -6.508  -15.253 1.442   0.50 8.68   ? 103 GLN A CG  1 
ATOM   901  C  CG  B GLN A 1 103 ? -6.744  -15.069 0.922   0.50 9.12   ? 103 GLN A CG  1 
ATOM   902  C  CD  A GLN A 1 103 ? -7.859  -15.895 1.363   0.50 9.41   ? 103 GLN A CD  1 
ATOM   903  C  CD  B GLN A 1 103 ? -8.213  -15.489 0.850   0.50 13.97  ? 103 GLN A CD  1 
ATOM   904  O  OE1 A GLN A 1 103 ? -8.037  -16.927 0.706   0.50 10.98  ? 103 GLN A OE1 1 
ATOM   905  O  OE1 B GLN A 1 103 ? -8.977  -15.458 1.836   0.50 20.09  ? 103 GLN A OE1 1 
ATOM   906  N  NE2 A GLN A 1 103 ? -8.885  -15.232 1.946   0.50 9.92   ? 103 GLN A NE2 1 
ATOM   907  N  NE2 B GLN A 1 103 ? -8.687  -15.890 -0.318  0.50 19.17  ? 103 GLN A NE2 1 
ATOM   908  N  N   . GLY A 1 104 ? -4.473  -12.190 0.236   1.00 6.55   ? 104 GLY A N   1 
ATOM   909  C  CA  . GLY A 1 104 ? -4.153  -11.040 1.056   1.00 5.95   ? 104 GLY A CA  1 
ATOM   910  C  C   . GLY A 1 104 ? -3.734  -9.845  0.212   1.00 6.32   ? 104 GLY A C   1 
ATOM   911  O  O   . GLY A 1 104 ? -3.948  -8.711  0.581   1.00 6.92   ? 104 GLY A O   1 
ATOM   912  N  N   . SER A 1 105 ? -2.999  -10.128 -0.890  1.00 5.61   ? 105 SER A N   1 
ATOM   913  C  CA  . SER A 1 105 ? -2.575  -9.026  -1.742  1.00 5.90   ? 105 SER A CA  1 
ATOM   914  C  C   . SER A 1 105 ? -3.767  -8.471  -2.492  1.00 5.71   ? 105 SER A C   1 
ATOM   915  O  O   . SER A 1 105 ? -4.834  -9.135  -2.691  1.00 6.75   ? 105 SER A O   1 
ATOM   916  C  CB  . SER A 1 105 ? -1.439  -9.414  -2.668  1.00 5.77   ? 105 SER A CB  1 
ATOM   917  O  OG  . SER A 1 105 ? -1.855  -10.310 -3.674  1.00 6.31   ? 105 SER A OG  1 
ATOM   918  N  N   . GLU A 1 106 ? -3.668  -7.231  -2.914  1.00 5.18   ? 106 GLU A N   1 
ATOM   919  C  CA  . GLU A 1 106 ? -4.643  -6.491  -3.705  1.00 6.21   ? 106 GLU A CA  1 
ATOM   920  C  C   . GLU A 1 106 ? -4.317  -6.648  -5.171  1.00 6.04   ? 106 GLU A C   1 
ATOM   921  O  O   . GLU A 1 106 ? -5.098  -7.240  -5.969  1.00 6.35   ? 106 GLU A O   1 
ATOM   922  C  CB  . GLU A 1 106 ? -4.707  -5.032  -3.270  1.00 5.85   ? 106 GLU A CB  1 
ATOM   923  C  CG  . GLU A 1 106 ? -5.162  -4.901  -1.811  1.00 6.46   ? 106 GLU A CG  1 
ATOM   924  C  CD  . GLU A 1 106 ? -5.831  -3.627  -1.532  1.00 6.29   ? 106 GLU A CD  1 
ATOM   925  O  OE1 . GLU A 1 106 ? -5.266  -2.538  -1.793  1.00 6.62   ? 106 GLU A OE1 1 
ATOM   926  O  OE2 . GLU A 1 106 ? -6.984  -3.687  -1.029  1.00 7.68   ? 106 GLU A OE2 1 
ATOM   927  N  N   . HIS A 1 107 ? -3.100  -6.225  -5.610  1.00 5.88   ? 107 HIS A N   1 
ATOM   928  C  CA  . HIS A 1 107 ? -2.662  -6.619  -6.934  1.00 6.36   ? 107 HIS A CA  1 
ATOM   929  C  C   . HIS A 1 107 ? -2.347  -8.098  -6.931  1.00 6.58   ? 107 HIS A C   1 
ATOM   930  O  O   . HIS A 1 107 ? -2.065  -8.686  -5.932  1.00 6.52   ? 107 HIS A O   1 
ATOM   931  C  CB  . HIS A 1 107 ? -1.374  -5.812  -7.297  1.00 6.96   ? 107 HIS A CB  1 
ATOM   932  C  CG  . HIS A 1 107 ? -1.736  -4.366  -7.449  1.00 7.66   ? 107 HIS A CG  1 
ATOM   933  N  ND1 . HIS A 1 107 ? -1.673  -3.458  -6.362  1.00 6.64   ? 107 HIS A ND1 1 
ATOM   934  C  CD2 . HIS A 1 107 ? -2.151  -3.632  -8.507  1.00 9.11   ? 107 HIS A CD2 1 
ATOM   935  C  CE1 . HIS A 1 107 ? -2.155  -2.298  -6.801  1.00 7.49   ? 107 HIS A CE1 1 
ATOM   936  N  NE2 . HIS A 1 107 ? -2.451  -2.345  -8.104  1.00 6.71   ? 107 HIS A NE2 1 
ATOM   937  N  N   . THR A 1 108 ? -2.552  -8.684  -8.136  1.00 6.06   ? 108 THR A N   1 
ATOM   938  C  CA  . THR A 1 108 ? -2.130  -10.047 -8.420  1.00 6.13   ? 108 THR A CA  1 
ATOM   939  C  C   . THR A 1 108 ? -1.147  -10.020 -9.592  1.00 5.76   ? 108 THR A C   1 
ATOM   940  O  O   . THR A 1 108 ? -1.153  -9.087  -10.355 1.00 6.56   ? 108 THR A O   1 
ATOM   941  C  CB  . THR A 1 108 ? -3.368  -10.961 -8.627  1.00 6.95   ? 108 THR A CB  1 
ATOM   942  O  OG1 . THR A 1 108 ? -4.168  -10.436 -9.677  1.00 7.44   ? 108 THR A OG1 1 
ATOM   943  C  CG2 . THR A 1 108 ? -4.183  -10.986 -7.347  1.00 7.97   ? 108 THR A CG2 1 
ATOM   944  N  N   . VAL A 1 109 ? -0.398  -11.098 -9.732  1.00 6.26   ? 109 VAL A N   1 
ATOM   945  C  CA  . VAL A 1 109 ? 0.592   -11.219 -10.793 1.00 7.12   ? 109 VAL A CA  1 
ATOM   946  C  C   . VAL A 1 109 ? 0.244   -12.523 -11.552 1.00 6.87   ? 109 VAL A C   1 
ATOM   947  O  O   . VAL A 1 109 ? 0.396   -13.607 -10.995 1.00 7.61   ? 109 VAL A O   1 
ATOM   948  C  CB  . VAL A 1 109 ? 2.047   -11.226 -10.248 1.00 8.51   ? 109 VAL A CB  1 
ATOM   949  C  CG1 . VAL A 1 109 ? 3.076   -11.318 -11.409 1.00 9.59   ? 109 VAL A CG1 1 
ATOM   950  C  CG2 . VAL A 1 109 ? 2.287   -9.964  -9.454  1.00 8.78   ? 109 VAL A CG2 1 
ATOM   951  N  N   . ASP A 1 110 ? -0.218  -12.402 -12.801 1.00 7.26   ? 110 ASP A N   1 
ATOM   952  C  CA  . ASP A 1 110 ? -0.662  -13.602 -13.506 1.00 9.53   ? 110 ASP A CA  1 
ATOM   953  C  C   . ASP A 1 110 ? -1.644  -14.423 -12.626 1.00 10.05  ? 110 ASP A C   1 
ATOM   954  O  O   . ASP A 1 110 ? -1.593  -15.676 -12.603 1.00 10.47  ? 110 ASP A O   1 
ATOM   955  C  CB  . ASP A 1 110 ? 0.495   -14.421 -14.020 1.00 11.06  ? 110 ASP A CB  1 
ATOM   956  C  CG  . ASP A 1 110 ? 1.307   -13.671 -15.057 1.00 11.41  ? 110 ASP A CG  1 
ATOM   957  O  OD1 . ASP A 1 110 ? 0.809   -12.761 -15.690 1.00 15.07  ? 110 ASP A OD1 1 
ATOM   958  O  OD2 . ASP A 1 110 ? 2.511   -13.991 -15.160 1.00 14.75  ? 110 ASP A OD2 1 
ATOM   959  N  N   . LYS A 1 111 ? -2.499  -13.676 -11.921 1.00 8.18   ? 111 LYS A N   1 
ATOM   960  C  CA  . LYS A 1 111 ? -3.580  -14.179 -11.072 1.00 9.67   ? 111 LYS A CA  1 
ATOM   961  C  C   . LYS A 1 111 ? -3.062  -14.715 -9.753  1.00 8.12   ? 111 LYS A C   1 
ATOM   962  O  O   . LYS A 1 111 ? -3.853  -15.059 -8.899  1.00 10.10  ? 111 LYS A O   1 
ATOM   963  C  CB  . LYS A 1 111 ? -4.481  -15.240 -11.766 1.00 10.10  ? 111 LYS A CB  1 
ATOM   964  C  CG  . LYS A 1 111 ? -5.258  -14.685 -12.980 1.00 13.39  ? 111 LYS A CG  1 
ATOM   965  C  CD  . LYS A 1 111 ? -6.183  -13.484 -12.665 1.00 17.52  ? 111 LYS A CD  1 
ATOM   966  C  CE  . LYS A 1 111 ? -6.904  -12.846 -13.869 1.00 24.73  ? 111 LYS A CE  1 
ATOM   967  N  NZ  . LYS A 1 111 ? -8.097  -13.571 -14.176 1.00 25.94  ? 111 LYS A NZ  1 
ATOM   968  N  N   . LYS A 1 112 ? -1.730  -14.729 -9.525  1.00 7.78   ? 112 LYS A N   1 
ATOM   969  C  CA  . LYS A 1 112 ? -1.177  -15.144 -8.234  1.00 7.41   ? 112 LYS A CA  1 
ATOM   970  C  C   . LYS A 1 112 ? -1.500  -14.090 -7.194  1.00 7.20   ? 112 LYS A C   1 
ATOM   971  O  O   . LYS A 1 112 ? -1.205  -12.900 -7.394  1.00 7.01   ? 112 LYS A O   1 
ATOM   972  C  CB  . LYS A 1 112 ? 0.337   -15.302 -8.342  1.00 8.74   ? 112 LYS A CB  1 
ATOM   973  C  CG  . LYS A 1 112 ? 1.025   -15.712 -7.022  1.00 11.58  ? 112 LYS A CG  1 
ATOM   974  C  CD  . LYS A 1 112 ? 2.537   -15.718 -7.072  1.00 13.01  ? 112 LYS A CD  1 
ATOM   975  C  CE  . LYS A 1 112 ? 3.121   -15.897 -5.705  1.00 14.85  ? 112 LYS A CE  1 
ATOM   976  N  NZ  . LYS A 1 112 ? 2.977   -17.252 -5.168  1.00 21.44  ? 112 LYS A NZ  1 
ATOM   977  N  N   A LYS A 1 113 ? -2.076  -14.507 -6.054  0.50 8.39   ? 113 LYS A N   1 
ATOM   978  N  N   B LYS A 1 113 ? -2.000  -14.561 -6.042  0.50 8.38   ? 113 LYS A N   1 
ATOM   979  C  CA  A LYS A 1 113 ? -2.225  -13.683 -4.860  0.50 8.24   ? 113 LYS A CA  1 
ATOM   980  C  CA  B LYS A 1 113 ? -2.172  -13.775 -4.830  0.50 8.37   ? 113 LYS A CA  1 
ATOM   981  C  C   A LYS A 1 113 ? -1.087  -13.988 -3.897  0.50 7.11   ? 113 LYS A C   1 
ATOM   982  C  C   B LYS A 1 113 ? -0.972  -14.024 -3.914  0.50 7.27   ? 113 LYS A C   1 
ATOM   983  O  O   A LYS A 1 113 ? -0.843  -15.145 -3.585  0.50 7.70   ? 113 LYS A O   1 
ATOM   984  O  O   B LYS A 1 113 ? -0.449  -15.138 -3.746  0.50 10.92  ? 113 LYS A O   1 
ATOM   985  C  CB  A LYS A 1 113 ? -3.512  -14.035 -4.112  0.50 9.47   ? 113 LYS A CB  1 
ATOM   986  C  CB  B LYS A 1 113 ? -3.514  -14.054 -4.142  0.50 9.45   ? 113 LYS A CB  1 
ATOM   987  C  CG  A LYS A 1 113 ? -4.786  -13.794 -4.913  0.50 9.85   ? 113 LYS A CG  1 
ATOM   988  C  CG  B LYS A 1 113 ? -4.741  -13.778 -5.022  0.50 10.34  ? 113 LYS A CG  1 
ATOM   989  C  CD  A LYS A 1 113 ? -5.977  -14.503 -4.258  0.50 10.46  ? 113 LYS A CD  1 
ATOM   990  C  CD  B LYS A 1 113 ? -6.052  -14.255 -4.418  0.50 10.19  ? 113 LYS A CD  1 
ATOM   991  C  CE  A LYS A 1 113 ? -7.318  -14.002 -4.744  0.50 11.23  ? 113 LYS A CE  1 
ATOM   992  C  CE  B LYS A 1 113 ? -7.210  -13.618 -5.152  0.50 11.30  ? 113 LYS A CE  1 
ATOM   993  N  NZ  A LYS A 1 113 ? -7.653  -14.522 -6.089  0.50 10.85  ? 113 LYS A NZ  1 
ATOM   994  N  NZ  B LYS A 1 113 ? -8.470  -14.415 -4.965  0.50 12.50  ? 113 LYS A NZ  1 
ATOM   995  N  N   . TYR A 1 114 ? -0.532  -12.928 -3.325  1.00 5.92   ? 114 TYR A N   1 
ATOM   996  C  CA  . TYR A 1 114 ? 0.470   -13.040 -2.299  1.00 6.72   ? 114 TYR A CA  1 
ATOM   997  C  C   . TYR A 1 114 ? -0.208  -12.945 -0.935  1.00 5.80   ? 114 TYR A C   1 
ATOM   998  O  O   . TYR A 1 114 ? -1.393  -12.606 -0.824  1.00 7.11   ? 114 TYR A O   1 
ATOM   999  C  CB  . TYR A 1 114 ? 1.497   -11.884 -2.435  1.00 7.24   ? 114 TYR A CB  1 
ATOM   1000 C  CG  . TYR A 1 114 ? 2.438   -12.121 -3.586  1.00 6.90   ? 114 TYR A CG  1 
ATOM   1001 C  CD1 . TYR A 1 114 ? 2.198   -11.704 -4.872  1.00 8.09   ? 114 TYR A CD1 1 
ATOM   1002 C  CD2 . TYR A 1 114 ? 3.657   -12.756 -3.366  1.00 8.24   ? 114 TYR A CD2 1 
ATOM   1003 C  CE1 . TYR A 1 114 ? 3.117   -11.864 -5.887  1.00 11.00  ? 114 TYR A CE1 1 
ATOM   1004 C  CE2 . TYR A 1 114 ? 4.607   -12.943 -4.384  1.00 10.93  ? 114 TYR A CE2 1 
ATOM   1005 C  CZ  . TYR A 1 114 ? 4.300   -12.521 -5.645  1.00 10.94  ? 114 TYR A CZ  1 
ATOM   1006 O  OH  . TYR A 1 114 ? 5.228   -12.674 -6.658  1.00 16.58  ? 114 TYR A OH  1 
ATOM   1007 N  N   . ALA A 1 115 ? 0.521   -13.276 0.133   1.00 6.27   ? 115 ALA A N   1 
ATOM   1008 C  CA  . ALA A 1 115 ? 0.035   -13.288 1.477   1.00 6.57   ? 115 ALA A CA  1 
ATOM   1009 C  C   . ALA A 1 115 ? -0.388  -11.922 1.958   1.00 6.18   ? 115 ALA A C   1 
ATOM   1010 O  O   . ALA A 1 115 ? -1.212  -11.784 2.843   1.00 6.87   ? 115 ALA A O   1 
ATOM   1011 C  CB  . ALA A 1 115 ? 1.041   -13.935 2.356   1.00 7.81   ? 115 ALA A CB  1 
ATOM   1012 N  N   . ALA A 1 116 ? 0.325   -10.881 1.487   1.00 5.87   ? 116 ALA A N   1 
ATOM   1013 C  CA  . ALA A 1 116 ? 0.016   -9.540  1.924   1.00 6.54   ? 116 ALA A CA  1 
ATOM   1014 C  C   . ALA A 1 116 ? 0.599   -8.574  0.911   1.00 5.88   ? 116 ALA A C   1 
ATOM   1015 O  O   . ALA A 1 116 ? 1.344   -8.963  -0.003  1.00 6.91   ? 116 ALA A O   1 
ATOM   1016 C  CB  . ALA A 1 116 ? 0.581   -9.280  3.354   1.00 6.82   ? 116 ALA A CB  1 
ATOM   1017 N  N   . GLU A 1 117 ? 0.264   -7.288  1.082   1.00 6.28   ? 117 GLU A N   1 
ATOM   1018 C  CA  . GLU A 1 117 ? 0.792   -6.230  0.237   1.00 5.77   ? 117 GLU A CA  1 
ATOM   1019 C  C   . GLU A 1 117 ? 0.988   -4.971  1.085   1.00 6.12   ? 117 GLU A C   1 
ATOM   1020 O  O   . GLU A 1 117 ? 0.075   -4.617  1.833   1.00 7.04   ? 117 GLU A O   1 
ATOM   1021 C  CB  . GLU A 1 117 ? -0.170  -5.949  -0.921  1.00 6.65   ? 117 GLU A CB  1 
ATOM   1022 C  CG  . GLU A 1 117 ? 0.389   -5.018  -1.983  1.00 5.62   ? 117 GLU A CG  1 
ATOM   1023 C  CD  . GLU A 1 117 ? -0.469  -4.939  -3.206  1.00 5.18   ? 117 GLU A CD  1 
ATOM   1024 O  OE1 . GLU A 1 117 ? -1.131  -5.946  -3.536  1.00 6.63   ? 117 GLU A OE1 1 
ATOM   1025 O  OE2 . GLU A 1 117 ? -0.491  -3.869  -3.849  1.00 6.14   ? 117 GLU A OE2 1 
ATOM   1026 N  N   . LEU A 1 118 ? 2.184   -4.371  1.000   1.00 6.06   ? 118 LEU A N   1 
ATOM   1027 C  CA  . LEU A 1 118 ? 2.562   -3.146  1.650   1.00 5.77   ? 118 LEU A CA  1 
ATOM   1028 C  C   . LEU A 1 118 ? 2.313   -2.007  0.693   1.00 6.26   ? 118 LEU A C   1 
ATOM   1029 O  O   . LEU A 1 118 ? 2.762   -2.059  -0.461  1.00 6.59   ? 118 LEU A O   1 
ATOM   1030 C  CB  . LEU A 1 118 ? 4.067   -3.273  1.984   1.00 7.07   ? 118 LEU A CB  1 
ATOM   1031 C  CG  . LEU A 1 118 ? 4.784   -1.983  2.395   1.00 7.98   ? 118 LEU A CG  1 
ATOM   1032 C  CD1 . LEU A 1 118 ? 4.131   -1.316  3.611   1.00 9.51   ? 118 LEU A CD1 1 
ATOM   1033 C  CD2 . LEU A 1 118 ? 6.255   -2.332  2.699   1.00 9.59   ? 118 LEU A CD2 1 
ATOM   1034 N  N   . HIS A 1 119 ? 1.682   -0.948  1.183   1.00 6.19   ? 119 HIS A N   1 
ATOM   1035 C  CA  . HIS A 1 119 ? 1.473   0.274   0.409   1.00 6.04   ? 119 HIS A CA  1 
ATOM   1036 C  C   . HIS A 1 119 ? 2.107   1.446   1.123   1.00 5.38   ? 119 HIS A C   1 
ATOM   1037 O  O   . HIS A 1 119 ? 1.747   1.784   2.240   1.00 7.03   ? 119 HIS A O   1 
ATOM   1038 C  CB  . HIS A 1 119 ? -0.053  0.555   0.271   1.00 6.65   ? 119 HIS A CB  1 
ATOM   1039 C  CG  . HIS A 1 119 ? -0.702  -0.421  -0.667  1.00 6.25   ? 119 HIS A CG  1 
ATOM   1040 N  ND1 . HIS A 1 119 ? -2.090  -0.614  -0.706  1.00 5.86   ? 119 HIS A ND1 1 
ATOM   1041 C  CD2 . HIS A 1 119 ? -0.160  -1.211  -1.591  1.00 5.78   ? 119 HIS A CD2 1 
ATOM   1042 C  CE1 . HIS A 1 119 ? -2.350  -1.556  -1.583  1.00 5.32   ? 119 HIS A CE1 1 
ATOM   1043 N  NE2 . HIS A 1 119 ? -1.225  -1.891  -2.182  1.00 6.02   ? 119 HIS A NE2 1 
ATOM   1044 N  N   . LEU A 1 120 ? 3.070   2.066   0.437   1.00 6.61   ? 120 LEU A N   1 
ATOM   1045 C  CA  . LEU A 1 120 ? 3.689   3.323   0.909   1.00 8.20   ? 120 LEU A CA  1 
ATOM   1046 C  C   . LEU A 1 120 ? 3.070   4.452   0.098   1.00 8.61   ? 120 LEU A C   1 
ATOM   1047 O  O   . LEU A 1 120 ? 3.182   4.489   -1.133  1.00 7.56   ? 120 LEU A O   1 
ATOM   1048 C  CB  . LEU A 1 120 ? 5.209   3.255   0.687   1.00 9.29   ? 120 LEU A CB  1 
ATOM   1049 C  CG  . LEU A 1 120 ? 5.874   2.169   1.570   1.00 8.88   ? 120 LEU A CG  1 
ATOM   1050 C  CD1 . LEU A 1 120 ? 6.754   1.241   0.723   1.00 13.41  ? 120 LEU A CD1 1 
ATOM   1051 C  CD2 . LEU A 1 120 ? 6.723   2.892   2.662   1.00 11.39  ? 120 LEU A CD2 1 
ATOM   1052 N  N   . VAL A 1 121 ? 2.335   5.324   0.768   1.00 7.34   ? 121 VAL A N   1 
ATOM   1053 C  CA  . VAL A 1 121 ? 1.446   6.319   0.097   1.00 7.13   ? 121 VAL A CA  1 
ATOM   1054 C  C   . VAL A 1 121 ? 2.169   7.670   0.130   1.00 7.57   ? 121 VAL A C   1 
ATOM   1055 O  O   . VAL A 1 121 ? 2.628   8.132   1.214   1.00 9.79   ? 121 VAL A O   1 
ATOM   1056 C  CB  . VAL A 1 121 ? 0.095   6.411   0.813   1.00 8.03   ? 121 VAL A CB  1 
ATOM   1057 C  CG1 . VAL A 1 121 ? -0.816  7.450   0.191   1.00 7.95   ? 121 VAL A CG1 1 
ATOM   1058 C  CG2 . VAL A 1 121 ? -0.618  5.060   0.938   1.00 8.31   ? 121 VAL A CG2 1 
ATOM   1059 N  N   . HIS A 1 122 ? 2.257   8.297   -1.020  1.00 6.60   ? 122 HIS A N   1 
ATOM   1060 C  CA  . HIS A 1 122 ? 2.968   9.573   -1.185  1.00 7.46   ? 122 HIS A CA  1 
ATOM   1061 C  C   . HIS A 1 122 ? 2.064   10.535  -1.932  1.00 7.00   ? 122 HIS A C   1 
ATOM   1062 O  O   . HIS A 1 122 ? 1.270   10.135  -2.779  1.00 7.29   ? 122 HIS A O   1 
ATOM   1063 C  CB  . HIS A 1 122 ? 4.242   9.411   -2.011  1.00 8.85   ? 122 HIS A CB  1 
ATOM   1064 C  CG  . HIS A 1 122 ? 5.127   8.269   -1.624  1.00 9.11   ? 122 HIS A CG  1 
ATOM   1065 N  ND1 . HIS A 1 122 ? 4.776   6.966   -1.864  1.00 8.13   ? 122 HIS A ND1 1 
ATOM   1066 C  CD2 . HIS A 1 122 ? 6.366   8.228   -1.056  1.00 9.10   ? 122 HIS A CD2 1 
ATOM   1067 C  CE1 . HIS A 1 122 ? 5.772   6.172   -1.482  1.00 8.33   ? 122 HIS A CE1 1 
ATOM   1068 N  NE2 . HIS A 1 122 ? 6.786   6.926   -0.958  1.00 8.97   ? 122 HIS A NE2 1 
ATOM   1069 N  N   . TRP A 1 123 ? 2.203   11.834  -1.655  1.00 7.23   ? 123 TRP A N   1 
ATOM   1070 C  CA  . TRP A 1 123 ? 1.401   12.841  -2.347  1.00 7.20   ? 123 TRP A CA  1 
ATOM   1071 C  C   . TRP A 1 123 ? 2.296   13.853  -3.042  1.00 8.34   ? 123 TRP A C   1 
ATOM   1072 O  O   . TRP A 1 123 ? 3.402   14.206  -2.585  1.00 9.68   ? 123 TRP A O   1 
ATOM   1073 C  CB  . TRP A 1 123 ? 0.355   13.475  -1.426  1.00 9.25   ? 123 TRP A CB  1 
ATOM   1074 C  CG  . TRP A 1 123 ? 0.943   14.142  -0.210  1.00 11.60  ? 123 TRP A CG  1 
ATOM   1075 C  CD1 . TRP A 1 123 ? 1.215   13.561  0.997   1.00 15.49  ? 123 TRP A CD1 1 
ATOM   1076 C  CD2 . TRP A 1 123 ? 1.318   15.516  -0.061  1.00 11.69  ? 123 TRP A CD2 1 
ATOM   1077 N  NE1 . TRP A 1 123 ? 1.705   14.471  1.883   1.00 17.09  ? 123 TRP A NE1 1 
ATOM   1078 C  CE2 . TRP A 1 123 ? 1.771   15.683  1.256   1.00 15.30  ? 123 TRP A CE2 1 
ATOM   1079 C  CE3 . TRP A 1 123 ? 1.248   16.623  -0.893  1.00 11.26  ? 123 TRP A CE3 1 
ATOM   1080 C  CZ2 . TRP A 1 123 ? 2.230   16.901  1.740   1.00 14.96  ? 123 TRP A CZ2 1 
ATOM   1081 C  CZ3 . TRP A 1 123 ? 1.661   17.829  -0.401  1.00 13.96  ? 123 TRP A CZ3 1 
ATOM   1082 C  CH2 . TRP A 1 123 ? 2.174   17.962  0.895   1.00 16.38  ? 123 TRP A CH2 1 
ATOM   1083 N  N   . ASN A 1 124 ? 1.794   14.360  -4.160  1.00 7.35   ? 124 ASN A N   1 
ATOM   1084 C  CA  . ASN A 1 124 ? 2.528   15.278  -5.046  1.00 7.65   ? 124 ASN A CA  1 
ATOM   1085 C  C   . ASN A 1 124 ? 2.571   16.659  -4.427  1.00 8.01   ? 124 ASN A C   1 
ATOM   1086 O  O   . ASN A 1 124 ? 1.564   17.292  -4.255  1.00 7.77   ? 124 ASN A O   1 
ATOM   1087 C  CB  . ASN A 1 124 ? 1.730   15.258  -6.366  1.00 8.87   ? 124 ASN A CB  1 
ATOM   1088 C  CG  . ASN A 1 124 ? 2.478   15.955  -7.479  1.00 8.82   ? 124 ASN A CG  1 
ATOM   1089 O  OD1 . ASN A 1 124 ? 3.321   16.815  -7.273  1.00 9.89   ? 124 ASN A OD1 1 
ATOM   1090 N  ND2 . ASN A 1 124 ? 2.160   15.510  -8.712  1.00 10.16  ? 124 ASN A ND2 1 
ATOM   1091 N  N   . THR A 1 125 ? 3.813   17.129  -4.143  1.00 9.92   ? 125 THR A N   1 
ATOM   1092 C  CA  . THR A 1 125 ? 4.001   18.421  -3.452  1.00 11.23  ? 125 THR A CA  1 
ATOM   1093 C  C   . THR A 1 125 ? 3.462   19.562  -4.270  1.00 12.23  ? 125 THR A C   1 
ATOM   1094 O  O   . THR A 1 125 ? 3.219   20.613  -3.707  1.00 13.03  ? 125 THR A O   1 
ATOM   1095 C  CB  . THR A 1 125 ? 5.444   18.638  -2.988  1.00 15.51  ? 125 THR A CB  1 
ATOM   1096 O  OG1 . THR A 1 125 ? 6.327   18.669  -4.202  1.00 22.49  ? 125 THR A OG1 1 
ATOM   1097 C  CG2 . THR A 1 125 ? 5.876   17.496  -2.076  1.00 17.32  ? 125 THR A CG2 1 
ATOM   1098 N  N   . LYS A 1 126 ? 3.292   19.411  -5.600  1.00 11.15  ? 126 LYS A N   1 
ATOM   1099 C  CA  . LYS A 1 126 ? 2.718   20.514  -6.365  1.00 13.08  ? 126 LYS A CA  1 
ATOM   1100 C  C   . LYS A 1 126 ? 1.326   20.910  -5.903  1.00 12.86  ? 126 LYS A C   1 
ATOM   1101 O  O   . LYS A 1 126 ? 0.922   22.070  -6.158  1.00 16.15  ? 126 LYS A O   1 
ATOM   1102 C  CB  . LYS A 1 126 ? 2.900   20.400  -7.864  1.00 16.28  ? 126 LYS A CB  1 
ATOM   1103 C  CG  . LYS A 1 126 ? 1.933   19.456  -8.545  1.00 16.26  ? 126 LYS A CG  1 
ATOM   1104 C  CD  . LYS A 1 126 ? 2.225   19.506  -10.045 1.00 27.08  ? 126 LYS A CD  1 
ATOM   1105 C  CE  . LYS A 1 126 ? 1.554   18.468  -10.910 1.00 33.03  ? 126 LYS A CE  1 
ATOM   1106 N  NZ  . LYS A 1 126 ? 0.444   19.003  -11.732 1.00 37.84  ? 126 LYS A NZ  1 
ATOM   1107 N  N   . TYR A 1 127 ? 0.614   20.022  -5.206  1.00 9.76   ? 127 TYR A N   1 
ATOM   1108 C  CA  . TYR A 1 127 ? -0.735  20.313  -4.747  1.00 9.51   ? 127 TYR A CA  1 
ATOM   1109 C  C   . TYR A 1 127 ? -0.806  20.765  -3.266  1.00 9.44   ? 127 TYR A C   1 
ATOM   1110 O  O   . TYR A 1 127 ? -1.898  21.043  -2.754  1.00 10.46  ? 127 TYR A O   1 
ATOM   1111 C  CB  . TYR A 1 127 ? -1.649  19.116  -5.030  1.00 10.37  ? 127 TYR A CB  1 
ATOM   1112 C  CG  . TYR A 1 127 ? -1.752  18.805  -6.498  1.00 10.69  ? 127 TYR A CG  1 
ATOM   1113 C  CD1 . TYR A 1 127 ? -2.088  19.773  -7.446  1.00 10.60  ? 127 TYR A CD1 1 
ATOM   1114 C  CD2 . TYR A 1 127 ? -1.444  17.517  -6.986  1.00 8.92   ? 127 TYR A CD2 1 
ATOM   1115 C  CE1 . TYR A 1 127 ? -2.134  19.454  -8.798  1.00 11.54  ? 127 TYR A CE1 1 
ATOM   1116 C  CE2 . TYR A 1 127 ? -1.383  17.245  -8.324  1.00 10.45  ? 127 TYR A CE2 1 
ATOM   1117 C  CZ  . TYR A 1 127 ? -1.809  18.204  -9.243  1.00 10.73  ? 127 TYR A CZ  1 
ATOM   1118 O  OH  . TYR A 1 127 ? -1.769  17.966  -10.554 1.00 14.16  ? 127 TYR A OH  1 
ATOM   1119 N  N   . GLY A 1 128 ? 0.355   20.819  -2.589  1.00 10.67  ? 128 GLY A N   1 
ATOM   1120 C  CA  . GLY A 1 128 ? 0.352   21.483  -1.296  1.00 11.31  ? 128 GLY A CA  1 
ATOM   1121 C  C   . GLY A 1 128 ? -0.055  20.648  -0.087  1.00 10.46  ? 128 GLY A C   1 
ATOM   1122 O  O   . GLY A 1 128 ? 0.493   20.789  1.009   1.00 12.08  ? 128 GLY A O   1 
ATOM   1123 N  N   . ASP A 1 129 ? -1.128  19.874  -0.219  1.00 9.97   ? 129 ASP A N   1 
ATOM   1124 C  CA  . ASP A 1 129 ? -1.623  19.046  0.875   1.00 11.70  ? 129 ASP A CA  1 
ATOM   1125 C  C   . ASP A 1 129 ? -2.335  17.834  0.297   1.00 8.97   ? 129 ASP A C   1 
ATOM   1126 O  O   . ASP A 1 129 ? -2.724  17.826  -0.899  1.00 10.75  ? 129 ASP A O   1 
ATOM   1127 C  CB  . ASP A 1 129 ? -2.550  19.805  1.857   1.00 10.65  ? 129 ASP A CB  1 
ATOM   1128 C  CG  . ASP A 1 129 ? -3.912  20.223  1.340   1.00 12.90  ? 129 ASP A CG  1 
ATOM   1129 O  OD1 . ASP A 1 129 ? -4.795  19.375  1.087   1.00 16.10  ? 129 ASP A OD1 1 
ATOM   1130 O  OD2 . ASP A 1 129 ? -4.135  21.415  1.348   1.00 17.57  ? 129 ASP A OD2 1 
ATOM   1131 N  N   A VAL A 1 130 ? -2.560  16.795  1.111   0.50 9.69   ? 130 VAL A N   1 
ATOM   1132 N  N   B VAL A 1 130 ? -2.440  16.793  1.127   0.50 11.82  ? 130 VAL A N   1 
ATOM   1133 C  CA  A VAL A 1 130 ? -3.055  15.511  0.603   0.50 10.92  ? 130 VAL A CA  1 
ATOM   1134 C  CA  B VAL A 1 130 ? -3.029  15.534  0.682   0.50 13.51  ? 130 VAL A CA  1 
ATOM   1135 C  C   A VAL A 1 130 ? -4.521  15.585  0.222   0.50 9.03   ? 130 VAL A C   1 
ATOM   1136 C  C   B VAL A 1 130 ? -4.421  15.754  0.128   0.50 12.15  ? 130 VAL A C   1 
ATOM   1137 O  O   A VAL A 1 130 ? -4.957  14.881  -0.658  0.50 6.46   ? 130 VAL A O   1 
ATOM   1138 O  O   B VAL A 1 130 ? -4.684  15.303  -0.971  0.50 8.58   ? 130 VAL A O   1 
ATOM   1139 C  CB  A VAL A 1 130 ? -2.749  14.357  1.579   0.50 10.23  ? 130 VAL A CB  1 
ATOM   1140 C  CB  B VAL A 1 130 ? -2.950  14.418  1.743   0.50 14.78  ? 130 VAL A CB  1 
ATOM   1141 C  CG1 A VAL A 1 130 ? -3.674  14.435  2.812   0.50 11.44  ? 130 VAL A CG1 1 
ATOM   1142 C  CG1 B VAL A 1 130 ? -3.700  13.161  1.306   0.50 14.47  ? 130 VAL A CG1 1 
ATOM   1143 C  CG2 A VAL A 1 130 ? -2.905  12.990  0.872   0.50 9.73   ? 130 VAL A CG2 1 
ATOM   1144 C  CG2 B VAL A 1 130 ? -1.493  14.090  2.057   0.50 16.76  ? 130 VAL A CG2 1 
ATOM   1145 N  N   . GLY A 1 131 ? -5.295  16.431  0.907   1.00 12.16  ? 131 GLY A N   1 
ATOM   1146 C  CA  . GLY A 1 131 ? -6.665  16.634  0.523   1.00 12.52  ? 131 GLY A CA  1 
ATOM   1147 C  C   . GLY A 1 131 ? -6.833  17.222  -0.875  1.00 9.50   ? 131 GLY A C   1 
ATOM   1148 O  O   . GLY A 1 131 ? -7.700  16.778  -1.656  1.00 10.34  ? 131 GLY A O   1 
ATOM   1149 N  N   . LYS A 1 132 ? -5.949  18.158  -1.261  1.00 9.66   ? 132 LYS A N   1 
ATOM   1150 C  CA  . LYS A 1 132 ? -5.994  18.701  -2.621  1.00 9.17   ? 132 LYS A CA  1 
ATOM   1151 C  C   . LYS A 1 132 ? -5.434  17.661  -3.611  1.00 8.07   ? 132 LYS A C   1 
ATOM   1152 O  O   . LYS A 1 132 ? -5.978  17.543  -4.690  1.00 8.23   ? 132 LYS A O   1 
ATOM   1153 C  CB  . LYS A 1 132 ? -5.192  20.024  -2.679  1.00 9.22   ? 132 LYS A CB  1 
ATOM   1154 C  CG  . LYS A 1 132 ? -5.900  21.179  -1.996  1.00 14.78  ? 132 LYS A CG  1 
ATOM   1155 C  CD  . LYS A 1 132 ? -7.160  21.705  -2.742  1.00 17.47  ? 132 LYS A CD  1 
ATOM   1156 C  CE  . LYS A 1 132 ? -7.725  22.932  -2.005  1.00 24.49  ? 132 LYS A CE  1 
ATOM   1157 N  NZ  . LYS A 1 132 ? -8.682  23.778  -2.785  1.00 38.70  ? 132 LYS A NZ  1 
ATOM   1158 N  N   . ALA A 1 133 ? -4.402  16.906  -3.211  1.00 7.83   ? 133 ALA A N   1 
ATOM   1159 C  CA  . ALA A 1 133 ? -3.837  15.909  -4.127  1.00 7.81   ? 133 ALA A CA  1 
ATOM   1160 C  C   . ALA A 1 133 ? -4.882  14.839  -4.450  1.00 7.57   ? 133 ALA A C   1 
ATOM   1161 O  O   . ALA A 1 133 ? -4.885  14.315  -5.558  1.00 7.82   ? 133 ALA A O   1 
ATOM   1162 C  CB  . ALA A 1 133 ? -2.608  15.290  -3.460  1.00 7.85   ? 133 ALA A CB  1 
ATOM   1163 N  N   . LEU A 1 134 ? -5.759  14.488  -3.500  1.00 7.68   ? 134 LEU A N   1 
ATOM   1164 C  CA  . LEU A 1 134 ? -6.802  13.465  -3.753  1.00 7.67   ? 134 LEU A CA  1 
ATOM   1165 C  C   . LEU A 1 134 ? -7.751  13.809  -4.902  1.00 8.57   ? 134 LEU A C   1 
ATOM   1166 O  O   . LEU A 1 134 ? -8.457  12.931  -5.415  1.00 9.23   ? 134 LEU A O   1 
ATOM   1167 C  CB  . LEU A 1 134 ? -7.612  13.250  -2.457  1.00 9.39   ? 134 LEU A CB  1 
ATOM   1168 C  CG  . LEU A 1 134 ? -6.937  12.475  -1.344  1.00 11.57  ? 134 LEU A CG  1 
ATOM   1169 C  CD1 . LEU A 1 134 ? -7.790  12.460  -0.101  1.00 17.62  ? 134 LEU A CD1 1 
ATOM   1170 C  CD2 . LEU A 1 134 ? -6.676  10.990  -1.669  1.00 12.76  ? 134 LEU A CD2 1 
ATOM   1171 N  N   . GLN A 1 135 ? -7.831  15.085  -5.234  1.00 7.93   ? 135 GLN A N   1 
ATOM   1172 C  CA  . GLN A 1 135 ? -8.689  15.630  -6.247  1.00 9.56   ? 135 GLN A CA  1 
ATOM   1173 C  C   . GLN A 1 135 ? -8.031  15.706  -7.604  1.00 8.50   ? 135 GLN A C   1 
ATOM   1174 O  O   . GLN A 1 135 ? -8.642  16.227  -8.525  1.00 11.22  ? 135 GLN A O   1 
ATOM   1175 C  CB  . GLN A 1 135 ? -9.271  17.002  -5.807  1.00 9.94   ? 135 GLN A CB  1 
ATOM   1176 C  CG  . GLN A 1 135 ? -9.919  16.914  -4.446  1.00 13.06  ? 135 GLN A CG  1 
ATOM   1177 C  CD  . GLN A 1 135 ? -10.460 18.239  -3.999  1.00 20.24  ? 135 GLN A CD  1 
ATOM   1178 O  OE1 . GLN A 1 135 ? -11.388 18.749  -4.605  1.00 26.34  ? 135 GLN A OE1 1 
ATOM   1179 N  NE2 . GLN A 1 135 ? -9.823  18.811  -2.989  1.00 23.16  ? 135 GLN A NE2 1 
ATOM   1180 N  N   A GLN A 1 136 ? -6.800  15.182  -7.753  0.50 8.11   ? 136 GLN A N   1 
ATOM   1181 N  N   B GLN A 1 136 ? -6.808  15.158  -7.740  0.50 8.29   ? 136 GLN A N   1 
ATOM   1182 C  CA  A GLN A 1 136 ? -6.104  15.321  -9.016  0.50 8.02   ? 136 GLN A CA  1 
ATOM   1183 C  CA  B GLN A 1 136 ? -6.076  15.303  -8.978  0.50 8.35   ? 136 GLN A CA  1 
ATOM   1184 C  C   A GLN A 1 136 ? -5.697  13.968  -9.547  0.50 8.02   ? 136 GLN A C   1 
ATOM   1185 C  C   B GLN A 1 136 ? -5.664  13.956  -9.543  0.50 8.26   ? 136 GLN A C   1 
ATOM   1186 O  O   A GLN A 1 136 ? -5.375  13.073  -8.764  0.50 8.02   ? 136 GLN A O   1 
ATOM   1187 O  O   B GLN A 1 136 ? -5.285  13.047  -8.799  0.50 9.24   ? 136 GLN A O   1 
ATOM   1188 C  CB  A GLN A 1 136 ? -4.762  16.057  -8.804  0.50 8.66   ? 136 GLN A CB  1 
ATOM   1189 C  CB  B GLN A 1 136 ? -4.816  16.151  -8.697  0.50 10.06  ? 136 GLN A CB  1 
ATOM   1190 C  CG  A GLN A 1 136 ? -4.870  17.234  -7.834  0.50 11.13  ? 136 GLN A CG  1 
ATOM   1191 C  CG  B GLN A 1 136 ? -5.150  17.517  -8.092  0.50 11.80  ? 136 GLN A CG  1 
ATOM   1192 C  CD  A GLN A 1 136 ? -5.827  18.295  -8.295  0.50 8.00   ? 136 GLN A CD  1 
ATOM   1193 C  CD  B GLN A 1 136 ? -5.680  18.424  -9.153  0.50 13.43  ? 136 GLN A CD  1 
ATOM   1194 O  OE1 A GLN A 1 136 ? -6.081  18.498  -9.503  0.50 10.51  ? 136 GLN A OE1 1 
ATOM   1195 O  OE1 B GLN A 1 136 ? -5.488  18.187  -10.340 0.50 16.77  ? 136 GLN A OE1 1 
ATOM   1196 N  NE2 A GLN A 1 136 ? -6.530  18.859  -7.339  0.50 12.01  ? 136 GLN A NE2 1 
ATOM   1197 N  NE2 B GLN A 1 136 ? -6.411  19.440  -8.708  0.50 17.88  ? 136 GLN A NE2 1 
ATOM   1198 N  N   . PRO A 1 137 ? -5.656  13.812  -10.893 1.00 7.49   ? 137 PRO A N   1 
ATOM   1199 C  CA  . PRO A 1 137 ? -5.326  12.510  -11.497 1.00 7.52   ? 137 PRO A CA  1 
ATOM   1200 C  C   . PRO A 1 137 ? -3.890  12.055  -11.230 1.00 7.77   ? 137 PRO A C   1 
ATOM   1201 O  O   . PRO A 1 137 ? -3.629  10.833  -11.312 1.00 10.48  ? 137 PRO A O   1 
ATOM   1202 C  CB  . PRO A 1 137 ? -5.542  12.731  -12.993 1.00 9.55   ? 137 PRO A CB  1 
ATOM   1203 C  CG  . PRO A 1 137 ? -5.503  14.211  -13.174 1.00 12.96  ? 137 PRO A CG  1 
ATOM   1204 C  CD  . PRO A 1 137 ? -6.110  14.777  -11.891 1.00 10.59  ? 137 PRO A CD  1 
ATOM   1205 N  N   . ASP A 1 138 ? -3.038  13.011  -10.906 1.00 7.67   ? 138 ASP A N   1 
ATOM   1206 C  CA  . ASP A 1 138 ? -1.638  12.668  -10.565 1.00 9.35   ? 138 ASP A CA  1 
ATOM   1207 C  C   . ASP A 1 138 ? -1.319  13.162  -9.147  1.00 7.76   ? 138 ASP A C   1 
ATOM   1208 O  O   . ASP A 1 138 ? -0.187  13.580  -8.869  1.00 9.31   ? 138 ASP A O   1 
ATOM   1209 C  CB  . ASP A 1 138 ? -0.653  13.284  -11.567 1.00 10.48  ? 138 ASP A CB  1 
ATOM   1210 C  CG  . ASP A 1 138 ? -0.771  14.780  -11.694 1.00 11.58  ? 138 ASP A CG  1 
ATOM   1211 O  OD1 . ASP A 1 138 ? -1.675  15.384  -11.074 1.00 11.44  ? 138 ASP A OD1 1 
ATOM   1212 O  OD2 . ASP A 1 138 ? 0.113   15.349  -12.389 1.00 14.97  ? 138 ASP A OD2 1 
ATOM   1213 N  N   . GLY A 1 139 ? -2.296  13.082  -8.243  1.00 6.93   ? 139 GLY A N   1 
ATOM   1214 C  CA  . GLY A 1 139 ? -2.111  13.541  -6.899  1.00 7.36   ? 139 GLY A CA  1 
ATOM   1215 C  C   . GLY A 1 139 ? -1.245  12.652  -6.021  1.00 6.32   ? 139 GLY A C   1 
ATOM   1216 O  O   . GLY A 1 139 ? -0.586  13.182  -5.111  1.00 7.28   ? 139 GLY A O   1 
ATOM   1217 N  N   A LEU A 1 140 ? -1.373  11.326  -6.176  0.50 7.95   ? 140 LEU A N   1 
ATOM   1218 N  N   B LEU A 1 140 ? -1.414  11.328  -6.117  0.50 8.10   ? 140 LEU A N   1 
ATOM   1219 C  CA  A LEU A 1 140 ? -0.751  10.382  -5.253  0.50 7.57   ? 140 LEU A CA  1 
ATOM   1220 C  CA  B LEU A 1 140 ? -0.749  10.381  -5.225  0.50 7.59   ? 140 LEU A CA  1 
ATOM   1221 C  C   A LEU A 1 140 ? 0.098   9.400   -6.037  0.50 6.69   ? 140 LEU A C   1 
ATOM   1222 C  C   B LEU A 1 140 ? 0.097   9.394   -6.007  0.50 6.71   ? 140 LEU A C   1 
ATOM   1223 O  O   A LEU A 1 140 ? -0.181  9.177   -7.218  0.50 7.32   ? 140 LEU A O   1 
ATOM   1224 O  O   B LEU A 1 140 ? -0.192  9.096   -7.146  0.50 7.22   ? 140 LEU A O   1 
ATOM   1225 C  CB  A LEU A 1 140 ? -1.833  9.626   -4.463  0.50 9.07   ? 140 LEU A CB  1 
ATOM   1226 C  CB  B LEU A 1 140 ? -1.766  9.572   -4.412  0.50 8.89   ? 140 LEU A CB  1 
ATOM   1227 C  CG  A LEU A 1 140 ? -2.339  10.211  -3.124  0.50 11.16  ? 140 LEU A CG  1 
ATOM   1228 C  CG  B LEU A 1 140 ? -2.561  10.297  -3.321  0.50 10.42  ? 140 LEU A CG  1 
ATOM   1229 C  CD1 A LEU A 1 140 ? -3.031  11.565  -3.256  0.50 11.61  ? 140 LEU A CD1 1 
ATOM   1230 C  CD1 B LEU A 1 140 ? -3.275  9.279   -2.416  0.50 12.20  ? 140 LEU A CD1 1 
ATOM   1231 C  CD2 A LEU A 1 140 ? -3.257  9.229   -2.398  0.50 11.05  ? 140 LEU A CD2 1 
ATOM   1232 C  CD2 B LEU A 1 140 ? -1.811  11.332  -2.518  0.50 10.73  ? 140 LEU A CD2 1 
ATOM   1233 N  N   . ALA A 1 141 ? 1.143   8.884   -5.351  1.00 6.75   ? 141 ALA A N   1 
ATOM   1234 C  CA  . ALA A 1 141 ? 1.877   7.768   -5.903  1.00 7.04   ? 141 ALA A CA  1 
ATOM   1235 C  C   . ALA A 1 141 ? 1.951   6.750   -4.783  1.00 6.49   ? 141 ALA A C   1 
ATOM   1236 O  O   . ALA A 1 141 ? 2.352   7.077   -3.634  1.00 6.95   ? 141 ALA A O   1 
ATOM   1237 C  CB  . ALA A 1 141 ? 3.282   8.201   -6.379  1.00 8.21   ? 141 ALA A CB  1 
ATOM   1238 N  N   . VAL A 1 142 ? 1.512   5.496   -5.098  1.00 6.35   ? 142 VAL A N   1 
ATOM   1239 C  CA  . VAL A 1 142 ? 1.574   4.445   -4.106  1.00 6.60   ? 142 VAL A CA  1 
ATOM   1240 C  C   . VAL A 1 142 ? 2.560   3.398   -4.562  1.00 6.29   ? 142 VAL A C   1 
ATOM   1241 O  O   . VAL A 1 142 ? 2.463   2.940   -5.695  1.00 6.46   ? 142 VAL A O   1 
ATOM   1242 C  CB  . VAL A 1 142 ? 0.172   3.840   -3.758  1.00 6.93   ? 142 VAL A CB  1 
ATOM   1243 C  CG1 . VAL A 1 142 ? 0.311   2.834   -2.647  1.00 7.58   ? 142 VAL A CG1 1 
ATOM   1244 C  CG2 . VAL A 1 142 ? -0.769  4.963   -3.333  1.00 8.88   ? 142 VAL A CG2 1 
ATOM   1245 N  N   . LEU A 1 143 ? 3.591   3.172   -3.719  1.00 6.26   ? 143 LEU A N   1 
ATOM   1246 C  CA  . LEU A 1 143 ? 4.517   2.090   -3.958  1.00 6.73   ? 143 LEU A CA  1 
ATOM   1247 C  C   . LEU A 1 143 ? 4.047   0.835   -3.267  1.00 5.70   ? 143 LEU A C   1 
ATOM   1248 O  O   . LEU A 1 143 ? 3.826   0.789   -2.071  1.00 6.29   ? 143 LEU A O   1 
ATOM   1249 C  CB  . LEU A 1 143 ? 5.873   2.580   -3.395  1.00 7.98   ? 143 LEU A CB  1 
ATOM   1250 C  CG  . LEU A 1 143 ? 7.042   1.600   -3.528  1.00 9.93   ? 143 LEU A CG  1 
ATOM   1251 C  CD1 . LEU A 1 143 ? 7.348   1.330   -4.983  1.00 10.37  ? 143 LEU A CD1 1 
ATOM   1252 C  CD2 . LEU A 1 143 ? 8.285   2.178   -2.798  1.00 11.60  ? 143 LEU A CD2 1 
ATOM   1253 N  N   . GLY A 1 144 ? 3.785   -0.189  -4.115  1.00 6.51   ? 144 GLY A N   1 
ATOM   1254 C  CA  . GLY A 1 144 ? 3.235   -1.437  -3.585  1.00 6.08   ? 144 GLY A CA  1 
ATOM   1255 C  C   . GLY A 1 144 ? 4.289   -2.540  -3.617  1.00 6.50   ? 144 GLY A C   1 
ATOM   1256 O  O   . GLY A 1 144 ? 5.014   -2.678  -4.590  1.00 6.19   ? 144 GLY A O   1 
ATOM   1257 N  N   . ILE A 1 145 ? 4.331   -3.287  -2.548  1.00 6.07   ? 145 ILE A N   1 
ATOM   1258 C  CA  . ILE A 1 145 ? 5.356   -4.319  -2.366  1.00 6.70   ? 145 ILE A CA  1 
ATOM   1259 C  C   . ILE A 1 145 ? 4.621   -5.569  -1.892  1.00 6.61   ? 145 ILE A C   1 
ATOM   1260 O  O   . ILE A 1 145 ? 3.925   -5.534  -0.867  1.00 6.68   ? 145 ILE A O   1 
ATOM   1261 C  CB  . ILE A 1 145 ? 6.434   -3.851  -1.359  1.00 8.38   ? 145 ILE A CB  1 
ATOM   1262 C  CG1 . ILE A 1 145 ? 7.101   -2.573  -1.874  1.00 11.60  ? 145 ILE A CG1 1 
ATOM   1263 C  CG2 . ILE A 1 145 ? 7.448   -4.942  -1.168  1.00 8.94   ? 145 ILE A CG2 1 
ATOM   1264 C  CD1 . ILE A 1 145 ? 8.096   -2.022  -0.884  1.00 11.66  ? 145 ILE A CD1 1 
ATOM   1265 N  N   . PHE A 1 146 ? 4.838   -6.684  -2.576  1.00 6.00   ? 146 PHE A N   1 
ATOM   1266 C  CA  . PHE A 1 146 ? 4.198   -7.950  -2.173  1.00 6.48   ? 146 PHE A CA  1 
ATOM   1267 C  C   . PHE A 1 146 ? 4.968   -8.584  -1.014  1.00 6.09   ? 146 PHE A C   1 
ATOM   1268 O  O   . PHE A 1 146 ? 6.222   -8.469  -0.938  1.00 7.71   ? 146 PHE A O   1 
ATOM   1269 C  CB  . PHE A 1 146 ? 4.218   -8.919  -3.360  1.00 6.21   ? 146 PHE A CB  1 
ATOM   1270 C  CG  . PHE A 1 146 ? 3.389   -8.432  -4.524  1.00 6.03   ? 146 PHE A CG  1 
ATOM   1271 C  CD1 . PHE A 1 146 ? 1.996   -8.254  -4.348  1.00 6.68   ? 146 PHE A CD1 1 
ATOM   1272 C  CD2 . PHE A 1 146 ? 3.930   -8.156  -5.752  1.00 5.95   ? 146 PHE A CD2 1 
ATOM   1273 C  CE1 . PHE A 1 146 ? 1.208   -7.875  -5.438  1.00 5.99   ? 146 PHE A CE1 1 
ATOM   1274 C  CE2 . PHE A 1 146 ? 3.161   -7.753  -6.836  1.00 6.86   ? 146 PHE A CE2 1 
ATOM   1275 C  CZ  . PHE A 1 146 ? 1.766   -7.662  -6.663  1.00 6.80   ? 146 PHE A CZ  1 
ATOM   1276 N  N   . LEU A 1 147 ? 4.255   -9.306  -0.146  1.00 6.36   ? 147 LEU A N   1 
ATOM   1277 C  CA  . LEU A 1 147 ? 4.887   -10.121 0.898   1.00 6.86   ? 147 LEU A CA  1 
ATOM   1278 C  C   . LEU A 1 147 ? 4.504   -11.585 0.658   1.00 6.76   ? 147 LEU A C   1 
ATOM   1279 O  O   . LEU A 1 147 ? 3.318   -11.935 0.442   1.00 7.48   ? 147 LEU A O   1 
ATOM   1280 C  CB  . LEU A 1 147 ? 4.230   -9.761  2.259   1.00 7.68   ? 147 LEU A CB  1 
ATOM   1281 C  CG  . LEU A 1 147 ? 4.804   -8.477  2.910   1.00 9.29   ? 147 LEU A CG  1 
ATOM   1282 C  CD1 . LEU A 1 147 ? 4.713   -7.127  2.091   1.00 7.99   ? 147 LEU A CD1 1 
ATOM   1283 C  CD2 . LEU A 1 147 ? 4.210   -8.305  4.298   1.00 8.48   ? 147 LEU A CD2 1 
ATOM   1284 N  N   . LYS A 1 148 ? 5.512   -12.444 0.688   1.00 7.00   ? 148 LYS A N   1 
ATOM   1285 C  CA  . LYS A 1 148 ? 5.402   -13.861 0.750   1.00 7.42   ? 148 LYS A CA  1 
ATOM   1286 C  C   . LYS A 1 148 ? 5.844   -14.397 2.072   1.00 7.81   ? 148 LYS A C   1 
ATOM   1287 O  O   . LYS A 1 148 ? 6.673   -13.754 2.731   1.00 9.48   ? 148 LYS A O   1 
ATOM   1288 C  CB  . LYS A 1 148 ? 6.130   -14.523 -0.439  1.00 9.36   ? 148 LYS A CB  1 
ATOM   1289 C  CG  . LYS A 1 148 ? 7.610   -14.373 -0.394  1.00 10.45  ? 148 LYS A CG  1 
ATOM   1290 C  CD  . LYS A 1 148 ? 8.251   -15.076 -1.608  1.00 13.98  ? 148 LYS A CD  1 
ATOM   1291 C  CE  . LYS A 1 148 ? 9.742   -15.168 -1.437  1.00 23.17  ? 148 LYS A CE  1 
ATOM   1292 N  NZ  . LYS A 1 148 ? 10.218  -16.090 -2.484  1.00 32.51  ? 148 LYS A NZ  1 
ATOM   1293 N  N   . VAL A 1 149 ? 5.358   -15.545 2.443   1.00 7.98   ? 149 VAL A N   1 
ATOM   1294 C  CA  . VAL A 1 149 ? 5.708   -16.118 3.728   1.00 9.11   ? 149 VAL A CA  1 
ATOM   1295 C  C   . VAL A 1 149 ? 6.888   -17.077 3.554   1.00 8.98   ? 149 VAL A C   1 
ATOM   1296 O  O   . VAL A 1 149 ? 6.797   -18.056 2.801   1.00 11.15  ? 149 VAL A O   1 
ATOM   1297 C  CB  . VAL A 1 149 ? 4.499   -16.806 4.387   1.00 10.14  ? 149 VAL A CB  1 
ATOM   1298 C  CG1 . VAL A 1 149 ? 4.828   -17.483 5.716   1.00 14.04  ? 149 VAL A CG1 1 
ATOM   1299 C  CG2 . VAL A 1 149 ? 3.384   -15.816 4.608   1.00 11.87  ? 149 VAL A CG2 1 
ATOM   1300 N  N   . GLY A 1 150 ? 7.968   -16.809 4.287   1.00 9.69   ? 150 GLY A N   1 
ATOM   1301 C  CA  . GLY A 1 150 ? 9.113   -17.716 4.295   1.00 12.93  ? 150 GLY A CA  1 
ATOM   1302 C  C   . GLY A 1 150 ? 10.005  -17.208 5.431   1.00 11.61  ? 150 GLY A C   1 
ATOM   1303 O  O   . GLY A 1 150 ? 9.647   -17.321 6.588   1.00 11.58  ? 150 GLY A O   1 
ATOM   1304 N  N   A SER A 1 151 ? 11.227  -16.761 5.119   0.50 11.60  ? 151 SER A N   1 
ATOM   1305 N  N   B SER A 1 151 ? 11.203  -16.680 5.085   0.50 12.54  ? 151 SER A N   1 
ATOM   1306 C  CA  A SER A 1 151 ? 12.039  -16.195 6.190   0.50 13.25  ? 151 SER A CA  1 
ATOM   1307 C  CA  B SER A 1 151 ? 12.128  -16.056 6.041   0.50 14.66  ? 151 SER A CA  1 
ATOM   1308 C  C   A SER A 1 151 ? 11.460  -14.878 6.704   0.50 12.78  ? 151 SER A C   1 
ATOM   1309 C  C   B SER A 1 151 ? 11.614  -14.733 6.609   0.50 12.15  ? 151 SER A C   1 
ATOM   1310 O  O   A SER A 1 151 ? 10.623  -14.240 6.071   0.50 9.33   ? 151 SER A O   1 
ATOM   1311 O  O   B SER A 1 151 ? 11.033  -13.912 5.898   0.50 11.29  ? 151 SER A O   1 
ATOM   1312 C  CB  A SER A 1 151 ? 13.458  -16.039 5.722   0.50 17.35  ? 151 SER A CB  1 
ATOM   1313 C  CB  B SER A 1 151 ? 13.460  -15.790 5.380   0.50 16.08  ? 151 SER A CB  1 
ATOM   1314 O  OG  A SER A 1 151 ? 13.563  -15.117 4.642   0.50 21.74  ? 151 SER A OG  1 
ATOM   1315 O  OG  B SER A 1 151 ? 14.068  -16.982 4.927   0.50 18.64  ? 151 SER A OG  1 
ATOM   1316 N  N   . ALA A 1 152 ? 11.907  -14.481 7.891   1.00 11.29  ? 152 ALA A N   1 
ATOM   1317 C  CA  . ALA A 1 152 ? 11.473  -13.222 8.480   1.00 12.26  ? 152 ALA A CA  1 
ATOM   1318 C  C   . ALA A 1 152 ? 12.112  -12.023 7.809   1.00 11.85  ? 152 ALA A C   1 
ATOM   1319 O  O   . ALA A 1 152 ? 13.238  -12.093 7.356   1.00 14.70  ? 152 ALA A O   1 
ATOM   1320 C  CB  . ALA A 1 152 ? 11.849  -13.221 9.954   1.00 15.02  ? 152 ALA A CB  1 
ATOM   1321 N  N   . LYS A 1 153 ? 11.416  -10.887 7.916   1.00 13.11  ? 153 LYS A N   1 
ATOM   1322 C  CA  . LYS A 1 153 ? 11.962  -9.661  7.433   1.00 12.95  ? 153 LYS A CA  1 
ATOM   1323 C  C   . LYS A 1 153 ? 12.400  -8.862  8.660   1.00 14.45  ? 153 LYS A C   1 
ATOM   1324 O  O   . LYS A 1 153 ? 11.575  -8.426  9.457   1.00 13.93  ? 153 LYS A O   1 
ATOM   1325 C  CB  . LYS A 1 153 ? 10.911  -8.844  6.705   1.00 13.52  ? 153 LYS A CB  1 
ATOM   1326 C  CG  . LYS A 1 153 ? 11.386  -7.573  6.048   1.00 15.16  ? 153 LYS A CG  1 
ATOM   1327 C  CD  . LYS A 1 153 ? 12.186  -7.875  4.878   1.00 15.96  ? 153 LYS A CD  1 
ATOM   1328 C  CE  . LYS A 1 153 ? 12.107  -6.671  3.985   1.00 15.96  ? 153 LYS A CE  1 
ATOM   1329 N  NZ  . LYS A 1 153 ? 13.146  -6.910  2.979   1.00 16.94  ? 153 LYS A NZ  1 
ATOM   1330 N  N   . PRO A 1 154 ? 13.708  -8.748  8.963   1.00 14.41  ? 154 PRO A N   1 
ATOM   1331 C  CA  . PRO A 1 154 ? 14.099  -8.171  10.253  1.00 16.38  ? 154 PRO A CA  1 
ATOM   1332 C  C   . PRO A 1 154 ? 13.636  -6.718  10.413  1.00 15.03  ? 154 PRO A C   1 
ATOM   1333 O  O   . PRO A 1 154 ? 13.244  -6.325  11.502  1.00 16.79  ? 154 PRO A O   1 
ATOM   1334 C  CB  . PRO A 1 154 ? 15.623  -8.268  10.173  1.00 15.95  ? 154 PRO A CB  1 
ATOM   1335 C  CG  . PRO A 1 154 ? 15.943  -9.404  9.195   1.00 17.84  ? 154 PRO A CG  1 
ATOM   1336 C  CD  . PRO A 1 154 ? 14.824  -9.308  8.185   1.00 15.25  ? 154 PRO A CD  1 
ATOM   1337 N  N   . GLY A 1 155 ? 13.561  -5.955  9.299   1.00 14.99  ? 155 GLY A N   1 
ATOM   1338 C  CA  . GLY A 1 155 ? 13.137  -4.545  9.298   1.00 17.67  ? 155 GLY A CA  1 
ATOM   1339 C  C   . GLY A 1 155 ? 11.634  -4.359  9.568   1.00 16.41  ? 155 GLY A C   1 
ATOM   1340 O  O   . GLY A 1 155 ? 11.163  -3.263  9.856   1.00 19.55  ? 155 GLY A O   1 
ATOM   1341 N  N   . LEU A 1 156 ? 10.901  -5.456  9.550   1.00 14.80  ? 156 LEU A N   1 
ATOM   1342 C  CA  . LEU A 1 156 ? 9.479   -5.455  9.887   1.00 14.84  ? 156 LEU A CA  1 
ATOM   1343 C  C   . LEU A 1 156 ? 9.258   -5.691  11.367  1.00 17.71  ? 156 LEU A C   1 
ATOM   1344 O  O   . LEU A 1 156 ? 8.170   -5.345  11.853  1.00 15.00  ? 156 LEU A O   1 
ATOM   1345 C  CB  . LEU A 1 156 ? 8.748   -6.531  9.079   1.00 15.03  ? 156 LEU A CB  1 
ATOM   1346 C  CG  . LEU A 1 156 ? 7.223   -6.639  9.245   1.00 14.73  ? 156 LEU A CG  1 
ATOM   1347 C  CD1 . LEU A 1 156 ? 6.497   -5.327  8.940   1.00 15.66  ? 156 LEU A CD1 1 
ATOM   1348 C  CD2 . LEU A 1 156 ? 6.579   -7.785  8.429   1.00 13.44  ? 156 LEU A CD2 1 
ATOM   1349 N  N   . GLN A 1 157 ? 10.267  -6.236  12.079  1.00 14.85  ? 157 GLN A N   1 
ATOM   1350 C  CA  . GLN A 1 157 ? 9.964   -6.666  13.440  1.00 17.04  ? 157 GLN A CA  1 
ATOM   1351 C  C   . GLN A 1 157 ? 9.485   -5.553  14.363  1.00 16.51  ? 157 GLN A C   1 
ATOM   1352 O  O   . GLN A 1 157 ? 8.668   -5.839  15.204  1.00 15.79  ? 157 GLN A O   1 
ATOM   1353 C  CB  . GLN A 1 157 ? 11.096  -7.498  14.041  1.00 17.73  ? 157 GLN A CB  1 
ATOM   1354 C  CG  . GLN A 1 157 ? 10.699  -8.311  15.284  1.00 21.83  ? 157 GLN A CG  1 
ATOM   1355 C  CD  . GLN A 1 157 ? 9.598   -9.328  15.067  1.00 20.99  ? 157 GLN A CD  1 
ATOM   1356 O  OE1 . GLN A 1 157 ? 9.408   -9.880  13.984  1.00 20.96  ? 157 GLN A OE1 1 
ATOM   1357 N  NE2 . GLN A 1 157 ? 8.782   -9.550  16.090  1.00 23.57  ? 157 GLN A NE2 1 
ATOM   1358 N  N   . LYS A 1 158 ? 10.075  -4.341  14.307  1.00 16.54  ? 158 LYS A N   1 
ATOM   1359 C  CA  . LYS A 1 158 ? 9.642   -3.261  15.191  1.00 18.30  ? 158 LYS A CA  1 
ATOM   1360 C  C   . LYS A 1 158 ? 8.148   -2.949  15.018  1.00 15.75  ? 158 LYS A C   1 
ATOM   1361 O  O   . LYS A 1 158 ? 7.498   -2.594  15.987  1.00 16.95  ? 158 LYS A O   1 
ATOM   1362 C  CB  . LYS A 1 158 ? 10.572  -2.045  15.007  1.00 18.99  ? 158 LYS A CB  1 
ATOM   1363 C  CG  . LYS A 1 158 ? 11.983  -2.157  15.623  1.00 28.28  ? 158 LYS A CG  1 
ATOM   1364 C  CD  . LYS A 1 158 ? 12.899  -0.924  15.514  1.00 40.48  ? 158 LYS A CD  1 
ATOM   1365 C  CE  . LYS A 1 158 ? 14.348  -1.160  15.952  1.00 48.98  ? 158 LYS A CE  1 
ATOM   1366 N  NZ  . LYS A 1 158 ? 15.211  0.066   15.974  1.00 32.87  ? 158 LYS A NZ  1 
ATOM   1367 N  N   . VAL A 1 159 ? 7.582   -3.169  13.821  1.00 16.00  ? 159 VAL A N   1 
ATOM   1368 C  CA  . VAL A 1 159 ? 6.195   -2.867  13.569  1.00 14.95  ? 159 VAL A CA  1 
ATOM   1369 C  C   . VAL A 1 159 ? 5.378   -3.992  14.205  1.00 15.47  ? 159 VAL A C   1 
ATOM   1370 O  O   . VAL A 1 159 ? 4.470   -3.733  14.974  1.00 16.07  ? 159 VAL A O   1 
ATOM   1371 C  CB  . VAL A 1 159 ? 5.925   -2.817  12.051  1.00 18.32  ? 159 VAL A CB  1 
ATOM   1372 C  CG1 . VAL A 1 159 ? 4.409   -2.866  11.778  1.00 19.15  ? 159 VAL A CG1 1 
ATOM   1373 C  CG2 . VAL A 1 159 ? 6.592   -1.640  11.364  1.00 19.71  ? 159 VAL A CG2 1 
ATOM   1374 N  N   . VAL A 1 160 ? 5.750   -5.252  13.952  1.00 15.50  ? 160 VAL A N   1 
ATOM   1375 C  CA  . VAL A 1 160 ? 4.939   -6.348  14.477  1.00 18.04  ? 160 VAL A CA  1 
ATOM   1376 C  C   . VAL A 1 160 ? 4.925   -6.287  15.995  1.00 17.45  ? 160 VAL A C   1 
ATOM   1377 O  O   . VAL A 1 160 ? 3.935   -6.627  16.615  1.00 17.96  ? 160 VAL A O   1 
ATOM   1378 C  CB  . VAL A 1 160 ? 5.525   -7.708  13.984  1.00 22.71  ? 160 VAL A CB  1 
ATOM   1379 C  CG1 . VAL A 1 160 ? 5.219   -8.953  14.844  1.00 23.12  ? 160 VAL A CG1 1 
ATOM   1380 C  CG2 . VAL A 1 160 ? 5.328   -7.911  12.483  1.00 23.82  ? 160 VAL A CG2 1 
ATOM   1381 N  N   . ASP A 1 161 ? 6.046   -5.889  16.627  1.00 17.19  ? 161 ASP A N   1 
ATOM   1382 C  CA  . ASP A 1 161 ? 6.075   -5.959  18.091  1.00 18.50  ? 161 ASP A CA  1 
ATOM   1383 C  C   . ASP A 1 161 ? 5.210   -4.923  18.826  1.00 23.05  ? 161 ASP A C   1 
ATOM   1384 O  O   . ASP A 1 161 ? 4.952   -5.047  20.035  1.00 24.35  ? 161 ASP A O   1 
ATOM   1385 C  CB  . ASP A 1 161 ? 7.516   -5.964  18.574  1.00 22.38  ? 161 ASP A CB  1 
ATOM   1386 C  CG  . ASP A 1 161 ? 8.186   -7.335  18.484  1.00 22.67  ? 161 ASP A CG  1 
ATOM   1387 O  OD1 . ASP A 1 161 ? 7.449   -8.403  18.540  1.00 26.48  ? 161 ASP A OD1 1 
ATOM   1388 O  OD2 . ASP A 1 161 ? 9.430   -7.378  18.304  1.00 29.52  ? 161 ASP A OD2 1 
ATOM   1389 N  N   . VAL A 1 162 ? 4.721   -3.911  18.121  1.00 20.89  ? 162 VAL A N   1 
ATOM   1390 C  CA  . VAL A 1 162 ? 3.893   -2.901  18.742  1.00 21.25  ? 162 VAL A CA  1 
ATOM   1391 C  C   . VAL A 1 162 ? 2.393   -3.181  18.516  1.00 20.04  ? 162 VAL A C   1 
ATOM   1392 O  O   . VAL A 1 162 ? 1.565   -2.496  19.095  1.00 22.36  ? 162 VAL A O   1 
ATOM   1393 C  CB  . VAL A 1 162 ? 4.331   -1.490  18.269  1.00 26.02  ? 162 VAL A CB  1 
ATOM   1394 C  CG1 . VAL A 1 162 ? 3.798   -1.171  16.876  1.00 26.26  ? 162 VAL A CG1 1 
ATOM   1395 C  CG2 . VAL A 1 162 ? 4.008   -0.356  19.249  1.00 37.88  ? 162 VAL A CG2 1 
ATOM   1396 N  N   . LEU A 1 163 ? 2.025   -4.204  17.711  1.00 21.19  ? 163 LEU A N   1 
ATOM   1397 C  CA  . LEU A 1 163 ? 0.641   -4.342  17.290  1.00 21.48  ? 163 LEU A CA  1 
ATOM   1398 C  C   . LEU A 1 163 ? -0.257  -4.719  18.475  1.00 21.34  ? 163 LEU A C   1 
ATOM   1399 O  O   . LEU A 1 163 ? -1.427  -4.357  18.519  1.00 20.79  ? 163 LEU A O   1 
ATOM   1400 C  CB  . LEU A 1 163 ? 0.545   -5.379  16.173  1.00 17.38  ? 163 LEU A CB  1 
ATOM   1401 C  CG  . LEU A 1 163 ? 1.217   -5.002  14.861  1.00 15.24  ? 163 LEU A CG  1 
ATOM   1402 C  CD1 . LEU A 1 163 ? 0.945   -6.115  13.847  1.00 15.17  ? 163 LEU A CD1 1 
ATOM   1403 C  CD2 . LEU A 1 163 ? 0.647   -3.677  14.334  1.00 16.83  ? 163 LEU A CD2 1 
ATOM   1404 N  N   . ASP A 1 164 ? 0.302   -5.411  19.453  1.00 23.27  ? 164 ASP A N   1 
ATOM   1405 C  CA  . ASP A 1 164 ? -0.535  -5.769  20.588  1.00 23.73  ? 164 ASP A CA  1 
ATOM   1406 C  C   . ASP A 1 164 ? -0.976  -4.531  21.393  1.00 26.22  ? 164 ASP A C   1 
ATOM   1407 O  O   . ASP A 1 164 ? -1.930  -4.639  22.185  1.00 28.52  ? 164 ASP A O   1 
ATOM   1408 C  CB  . ASP A 1 164 ? 0.225   -6.655  21.570  1.00 26.09  ? 164 ASP A CB  1 
ATOM   1409 C  CG  . ASP A 1 164 ? 1.204   -5.835  22.387  1.00 27.20  ? 164 ASP A CG  1 
ATOM   1410 O  OD1 . ASP A 1 164 ? 2.200   -5.339  21.820  1.00 38.94  ? 164 ASP A OD1 1 
ATOM   1411 O  OD2 . ASP A 1 164 ? 0.972   -5.681  23.588  1.00 37.99  ? 164 ASP A OD2 1 
ATOM   1412 N  N   . SER A 1 165 ? -0.309  -3.376  21.185  1.00 24.22  ? 165 SER A N   1 
ATOM   1413 C  CA  . SER A 1 165 ? -0.692  -2.131  21.868  1.00 26.58  ? 165 SER A CA  1 
ATOM   1414 C  C   . SER A 1 165 ? -1.698  -1.316  21.073  1.00 24.80  ? 165 SER A C   1 
ATOM   1415 O  O   . SER A 1 165 ? -2.119  -0.256  21.522  1.00 26.20  ? 165 SER A O   1 
ATOM   1416 C  CB  . SER A 1 165 ? 0.509   -1.277  22.142  1.00 33.25  ? 165 SER A CB  1 
ATOM   1417 O  OG  . SER A 1 165 ? 0.927   -0.623  20.947  1.00 34.10  ? 165 SER A OG  1 
ATOM   1418 N  N   . ILE A 1 166 ? -2.007  -1.776  19.858  1.00 22.10  ? 166 ILE A N   1 
ATOM   1419 C  CA  . ILE A 1 166 ? -2.996  -1.133  19.030  1.00 25.60  ? 166 ILE A CA  1 
ATOM   1420 C  C   . ILE A 1 166 ? -4.023  -2.146  18.537  1.00 22.13  ? 166 ILE A C   1 
ATOM   1421 O  O   . ILE A 1 166 ? -4.443  -2.144  17.372  1.00 23.20  ? 166 ILE A O   1 
ATOM   1422 C  CB  . ILE A 1 166 ? -2.381  -0.278  17.906  1.00 23.05  ? 166 ILE A CB  1 
ATOM   1423 C  CG1 . ILE A 1 166 ? -1.486  -1.086  16.982  1.00 21.52  ? 166 ILE A CG1 1 
ATOM   1424 C  CG2 . ILE A 1 166 ? -1.631  0.936   18.459  1.00 26.19  ? 166 ILE A CG2 1 
ATOM   1425 C  CD1 . ILE A 1 166 ? -1.547  -0.473  15.595  1.00 17.73  ? 166 ILE A CD1 1 
ATOM   1426 N  N   . LYS A 1 167 ? -4.404  -3.063  19.443  1.00 23.32  ? 167 LYS A N   1 
ATOM   1427 C  CA  . LYS A 1 167 ? -5.079  -4.265  18.987  1.00 22.62  ? 167 LYS A CA  1 
ATOM   1428 C  C   . LYS A 1 167 ? -6.319  -3.788  18.301  1.00 21.39  ? 167 LYS A C   1 
ATOM   1429 O  O   . LYS A 1 167 ? -6.863  -4.439  17.354  1.00 20.70  ? 167 LYS A O   1 
ATOM   1430 C  CB  . LYS A 1 167 ? -5.485  -5.160  20.159  1.00 25.75  ? 167 LYS A CB  1 
ATOM   1431 C  CG  . LYS A 1 167 ? -6.302  -6.392  19.789  1.00 24.37  ? 167 LYS A CG  1 
ATOM   1432 C  CD  . LYS A 1 167 ? -6.428  -7.400  20.934  1.00 29.66  ? 167 LYS A CD  1 
ATOM   1433 C  CE  . LYS A 1 167 ? -7.460  -8.475  20.669  1.00 35.41  ? 167 LYS A CE  1 
ATOM   1434 N  NZ  . LYS A 1 167 ? -7.448  -9.535  21.711  1.00 44.36  ? 167 LYS A NZ  1 
ATOM   1435 N  N   . THR A 1 168 ? -6.729  -2.627  18.848  1.00 13.40  ? 168 THR A N   1 
ATOM   1436 C  CA  . THR A 1 168 ? -8.021  -2.205  18.485  1.00 14.04  ? 168 THR A CA  1 
ATOM   1437 C  C   . THR A 1 168 ? -8.185  -0.763  17.876  1.00 8.44   ? 168 THR A C   1 
ATOM   1438 O  O   . THR A 1 168 ? -7.204  0.007   17.913  1.00 13.60  ? 168 THR A O   1 
ATOM   1439 C  CB  . THR A 1 168 ? -9.043  -2.275  19.662  1.00 17.35  ? 168 THR A CB  1 
ATOM   1440 O  OG1 . THR A 1 168 ? -8.468  -1.474  20.704  1.00 16.50  ? 168 THR A OG1 1 
ATOM   1441 C  CG2 . THR A 1 168 ? -9.373  -3.708  20.030  1.00 17.05  ? 168 THR A CG2 1 
ATOM   1442 N  N   . LYS A 1 169 ? -9.238  -0.708  17.061  1.00 13.30  ? 169 LYS A N   1 
ATOM   1443 C  CA  . LYS A 1 169 ? -9.485  0.465   16.223  1.00 14.23  ? 169 LYS A CA  1 
ATOM   1444 C  C   . LYS A 1 169 ? -9.457  1.807   16.974  1.00 14.11  ? 169 LYS A C   1 
ATOM   1445 O  O   . LYS A 1 169 ? -10.074 1.908   18.057  1.00 21.36  ? 169 LYS A O   1 
ATOM   1446 C  CB  . LYS A 1 169 ? -10.902 0.356   15.745  1.00 12.43  ? 169 LYS A CB  1 
ATOM   1447 C  CG  . LYS A 1 169 ? -11.443 1.565   14.967  1.00 19.98  ? 169 LYS A CG  1 
ATOM   1448 C  CD  . LYS A 1 169 ? -12.652 1.442   14.096  1.00 22.49  ? 169 LYS A CD  1 
ATOM   1449 C  CE  . LYS A 1 169 ? -13.867 0.712   14.547  1.00 25.55  ? 169 LYS A CE  1 
ATOM   1450 N  NZ  . LYS A 1 169 ? -14.421 1.353   15.754  1.00 44.58  ? 169 LYS A NZ  1 
ATOM   1451 N  N   . GLY A 1 170 ? -8.546  2.708   16.521  1.00 13.94  ? 170 GLY A N   1 
ATOM   1452 C  CA  . GLY A 1 170 ? -8.490  3.970   17.226  1.00 20.89  ? 170 GLY A CA  1 
ATOM   1453 C  C   . GLY A 1 170 ? -7.372  4.087   18.218  1.00 21.93  ? 170 GLY A C   1 
ATOM   1454 O  O   . GLY A 1 170 ? -7.115  5.151   18.646  1.00 26.21  ? 170 GLY A O   1 
ATOM   1455 N  N   . LYS A 1 171 ? -6.632  3.001   18.459  1.00 22.92  ? 171 LYS A N   1 
ATOM   1456 C  CA  . LYS A 1 171 ? -5.386  2.968   19.140  1.00 17.04  ? 171 LYS A CA  1 
ATOM   1457 C  C   . LYS A 1 171 ? -4.246  3.421   18.262  1.00 37.09  ? 171 LYS A C   1 
ATOM   1458 O  O   . LYS A 1 171 ? -4.184  2.983   17.118  1.00 23.47  ? 171 LYS A O   1 
ATOM   1459 C  CB  . LYS A 1 171 ? -5.133  1.583   19.708  1.00 15.05  ? 171 LYS A CB  1 
ATOM   1460 C  CG  . LYS A 1 171 ? -6.113  1.231   20.772  1.00 20.49  ? 171 LYS A CG  1 
ATOM   1461 C  CD  . LYS A 1 171 ? -5.660  0.136   21.768  1.00 35.74  ? 171 LYS A CD  1 
ATOM   1462 C  CE  . LYS A 1 171 ? -6.293  0.288   23.145  1.00 48.69  ? 171 LYS A CE  1 
ATOM   1463 N  NZ  . LYS A 1 171 ? -5.327  0.825   24.139  1.00 68.41  ? 171 LYS A NZ  1 
ATOM   1464 N  N   . SER A 1 172 ? -3.389  4.277   18.819  1.00 17.86  ? 172 SER A N   1 
ATOM   1465 C  CA  . SER A 1 172 ? -2.120  4.643   18.309  1.00 50.10  ? 172 SER A CA  1 
ATOM   1466 C  C   . SER A 1 172 ? -1.056  4.579   19.402  1.00 18.30  ? 172 SER A C   1 
ATOM   1467 O  O   . SER A 1 172 ? -1.360  4.542   20.664  1.00 25.02  ? 172 SER A O   1 
ATOM   1468 C  CB  . SER A 1 172 ? -2.249  6.086   17.833  1.00 21.71  ? 172 SER A CB  1 
ATOM   1469 O  OG  . SER A 1 172 ? -2.421  6.996   18.910  1.00 23.87  ? 172 SER A OG  1 
ATOM   1470 N  N   . ALA A 1 173 ? 0.190   4.778   18.887  1.00 140.75 ? 173 ALA A N   1 
ATOM   1471 C  CA  . ALA A 1 173 ? 1.392   4.865   19.715  1.00 80.07  ? 173 ALA A CA  1 
ATOM   1472 C  C   . ALA A 1 173 ? 2.496   5.567   18.977  1.00 51.67  ? 173 ALA A C   1 
ATOM   1473 O  O   . ALA A 1 173 ? 2.569   5.476   17.754  1.00 23.32  ? 173 ALA A O   1 
ATOM   1474 C  CB  . ALA A 1 173 ? 1.779   3.381   20.073  1.00 67.23  ? 173 ALA A CB  1 
ATOM   1475 N  N   . ASP A 1 174 ? 3.367   6.178   19.747  1.00 29.56  ? 174 ASP A N   1 
ATOM   1476 C  CA  . ASP A 1 174 ? 4.573   6.705   19.211  1.00 30.82  ? 174 ASP A CA  1 
ATOM   1477 C  C   . ASP A 1 174 ? 5.163   5.504   18.426  1.00 39.74  ? 174 ASP A C   1 
ATOM   1478 O  O   . ASP A 1 174 ? 5.179   4.287   18.795  1.00 63.84  ? 174 ASP A O   1 
ATOM   1479 C  CB  . ASP A 1 174 ? 5.355   7.330   20.373  1.00 45.24  ? 174 ASP A CB  1 
ATOM   1480 C  CG  . ASP A 1 174 ? 4.769   8.675   20.777  1.00 59.90  ? 174 ASP A CG  1 
ATOM   1481 O  OD1 . ASP A 1 174 ? 3.630   8.684   21.330  1.00 68.23  ? 174 ASP A OD1 1 
ATOM   1482 O  OD2 . ASP A 1 174 ? 5.435   9.696   20.501  1.00 84.20  ? 174 ASP A OD2 1 
ATOM   1483 N  N   . PHE A 1 175 ? 5.934   6.007   17.386  1.00 26.03  ? 175 PHE A N   1 
ATOM   1484 C  CA  . PHE A 1 175 ? 6.693   5.176   16.467  1.00 23.74  ? 175 PHE A CA  1 
ATOM   1485 C  C   . PHE A 1 175 ? 7.674   6.042   15.729  1.00 34.49  ? 175 PHE A C   1 
ATOM   1486 O  O   . PHE A 1 175 ? 7.472   6.281   14.543  1.00 43.92  ? 175 PHE A O   1 
ATOM   1487 C  CB  . PHE A 1 175 ? 5.667   4.457   15.576  1.00 23.32  ? 175 PHE A CB  1 
ATOM   1488 C  CG  . PHE A 1 175 ? 6.137   3.104   15.154  1.00 21.52  ? 175 PHE A CG  1 
ATOM   1489 C  CD1 . PHE A 1 175 ? 6.365   2.088   16.065  1.00 24.12  ? 175 PHE A CD1 1 
ATOM   1490 C  CD2 . PHE A 1 175 ? 6.410   2.905   13.837  1.00 20.24  ? 175 PHE A CD2 1 
ATOM   1491 C  CE1 . PHE A 1 175 ? 6.844   0.863   15.660  1.00 24.02  ? 175 PHE A CE1 1 
ATOM   1492 C  CE2 . PHE A 1 175 ? 6.919   1.701   13.422  1.00 22.63  ? 175 PHE A CE2 1 
ATOM   1493 C  CZ  . PHE A 1 175 ? 7.137   0.686   14.329  1.00 21.98  ? 175 PHE A CZ  1 
ATOM   1494 N  N   . THR A 1 176 ? 8.573   6.575   16.509  1.00 18.23  ? 176 THR A N   1 
ATOM   1495 C  CA  . THR A 1 176 ? 9.572   7.426   15.970  1.00 25.26  ? 176 THR A CA  1 
ATOM   1496 C  C   . THR A 1 176 ? 10.658  6.476   15.607  1.00 17.57  ? 176 THR A C   1 
ATOM   1497 O  O   . THR A 1 176 ? 10.738  5.326   16.128  1.00 21.17  ? 176 THR A O   1 
ATOM   1498 C  CB  . THR A 1 176 ? 9.845   8.407   17.106  1.00 30.70  ? 176 THR A CB  1 
ATOM   1499 O  OG1 . THR A 1 176 ? 10.076  7.665   18.327  1.00 34.23  ? 176 THR A OG1 1 
ATOM   1500 C  CG2 . THR A 1 176 ? 8.682   9.341   17.337  1.00 41.80  ? 176 THR A CG2 1 
ATOM   1501 N  N   . ASN A 1 177 ? 11.491  7.021   14.730  1.00 21.69  ? 177 ASN A N   1 
ATOM   1502 C  CA  . ASN A 1 177 ? 12.735  6.430   14.345  1.00 22.79  ? 177 ASN A CA  1 
ATOM   1503 C  C   . ASN A 1 177 ? 12.530  5.093   13.623  1.00 22.83  ? 177 ASN A C   1 
ATOM   1504 O  O   . ASN A 1 177 ? 13.431  4.261   13.683  1.00 26.51  ? 177 ASN A O   1 
ATOM   1505 C  CB  . ASN A 1 177 ? 13.614  6.336   15.591  1.00 24.01  ? 177 ASN A CB  1 
ATOM   1506 C  CG  . ASN A 1 177 ? 13.799  7.720   16.221  1.00 21.38  ? 177 ASN A CG  1 
ATOM   1507 O  OD1 . ASN A 1 177 ? 14.463  8.576   15.661  1.00 22.98  ? 177 ASN A OD1 1 
ATOM   1508 N  ND2 . ASN A 1 177 ? 13.201  7.979   17.387  1.00 20.54  ? 177 ASN A ND2 1 
ATOM   1509 N  N   . PHE A 1 178 ? 11.364  4.879   12.962  1.00 23.74  ? 178 PHE A N   1 
ATOM   1510 C  CA  . PHE A 1 178 ? 11.251  3.653   12.230  1.00 22.59  ? 178 PHE A CA  1 
ATOM   1511 C  C   . PHE A 1 178 ? 11.774  3.972   10.832  1.00 16.49  ? 178 PHE A C   1 
ATOM   1512 O  O   . PHE A 1 178 ? 11.317  4.905   10.196  1.00 19.98  ? 178 PHE A O   1 
ATOM   1513 C  CB  . PHE A 1 178 ? 9.799   3.163   12.134  1.00 21.34  ? 178 PHE A CB  1 
ATOM   1514 C  CG  . PHE A 1 178 ? 9.700   1.934   11.275  1.00 20.11  ? 178 PHE A CG  1 
ATOM   1515 C  CD1 . PHE A 1 178 ? 10.111  0.717   11.780  1.00 19.22  ? 178 PHE A CD1 1 
ATOM   1516 C  CD2 . PHE A 1 178 ? 9.258   2.003   9.946   1.00 16.20  ? 178 PHE A CD2 1 
ATOM   1517 C  CE1 . PHE A 1 178 ? 10.020  -0.419  10.998  1.00 20.60  ? 178 PHE A CE1 1 
ATOM   1518 C  CE2 . PHE A 1 178 ? 9.263   0.875   9.145   1.00 13.98  ? 178 PHE A CE2 1 
ATOM   1519 C  CZ  . PHE A 1 178 ? 9.604   -0.319  9.675   1.00 16.02  ? 178 PHE A CZ  1 
ATOM   1520 N  N   . ASP A 1 179 ? 12.583  3.077   10.281  1.00 17.32  ? 179 ASP A N   1 
ATOM   1521 C  CA  . ASP A 1 179 ? 13.192  3.289   8.976   1.00 16.56  ? 179 ASP A CA  1 
ATOM   1522 C  C   . ASP A 1 179 ? 12.515  2.419   7.926   1.00 15.89  ? 179 ASP A C   1 
ATOM   1523 O  O   . ASP A 1 179 ? 12.675  1.209   7.912   1.00 15.69  ? 179 ASP A O   1 
ATOM   1524 C  CB  . ASP A 1 179 ? 14.676  2.964   9.041   1.00 19.43  ? 179 ASP A CB  1 
ATOM   1525 C  CG  . ASP A 1 179 ? 15.440  3.412   7.822   1.00 21.26  ? 179 ASP A CG  1 
ATOM   1526 O  OD1 . ASP A 1 179 ? 14.879  3.595   6.734   1.00 18.02  ? 179 ASP A OD1 1 
ATOM   1527 O  OD2 . ASP A 1 179 ? 16.622  3.633   7.993   1.00 27.82  ? 179 ASP A OD2 1 
ATOM   1528 N  N   . PRO A 1 180 ? 11.712  3.024   7.038   1.00 13.74  ? 180 PRO A N   1 
ATOM   1529 C  CA  . PRO A 1 180 ? 10.993  2.214   6.041   1.00 14.06  ? 180 PRO A CA  1 
ATOM   1530 C  C   . PRO A 1 180 ? 11.915  1.579   4.997   1.00 12.50  ? 180 PRO A C   1 
ATOM   1531 O  O   . PRO A 1 180 ? 11.446  0.670   4.275   1.00 11.57  ? 180 PRO A O   1 
ATOM   1532 C  CB  . PRO A 1 180 ? 9.980   3.231   5.487   1.00 14.46  ? 180 PRO A CB  1 
ATOM   1533 C  CG  . PRO A 1 180 ? 10.717  4.564   5.566   1.00 15.25  ? 180 PRO A CG  1 
ATOM   1534 C  CD  . PRO A 1 180 ? 11.356  4.457   6.976   1.00 14.16  ? 180 PRO A CD  1 
ATOM   1535 N  N   . ARG A 1 181 ? 13.196  1.975   4.929   1.00 13.32  ? 181 ARG A N   1 
ATOM   1536 C  CA  . ARG A 1 181 ? 14.134  1.350   4.001   1.00 13.57  ? 181 ARG A CA  1 
ATOM   1537 C  C   . ARG A 1 181 ? 14.263  -0.137  4.313   1.00 14.17  ? 181 ARG A C   1 
ATOM   1538 O  O   . ARG A 1 181 ? 14.592  -0.922  3.404   1.00 15.62  ? 181 ARG A O   1 
ATOM   1539 C  CB  . ARG A 1 181 ? 15.503  2.047   4.021   1.00 14.17  ? 181 ARG A CB  1 
ATOM   1540 C  CG  . ARG A 1 181 ? 15.396  3.428   3.392   1.00 18.23  ? 181 ARG A CG  1 
ATOM   1541 C  CD  . ARG A 1 181 ? 16.710  4.207   3.527   1.00 19.45  ? 181 ARG A CD  1 
ATOM   1542 N  NE  . ARG A 1 181 ? 17.350  4.073   4.841   1.00 23.31  ? 181 ARG A NE  1 
ATOM   1543 C  CZ  . ARG A 1 181 ? 18.491  4.671   5.195   1.00 28.25  ? 181 ARG A CZ  1 
ATOM   1544 N  NH1 . ARG A 1 181 ? 19.127  5.452   4.333   1.00 29.53  ? 181 ARG A NH1 1 
ATOM   1545 N  NH2 . ARG A 1 181 ? 18.990  4.486   6.409   1.00 33.56  ? 181 ARG A NH2 1 
ATOM   1546 N  N   . GLY A 1 182 ? 13.975  -0.505  5.571   1.00 15.23  ? 182 GLY A N   1 
ATOM   1547 C  CA  . GLY A 1 182 ? 14.019  -1.883  6.054   1.00 15.92  ? 182 GLY A CA  1 
ATOM   1548 C  C   . GLY A 1 182 ? 12.950  -2.792  5.452   1.00 13.50  ? 182 GLY A C   1 
ATOM   1549 O  O   . GLY A 1 182 ? 13.009  -3.990  5.706   1.00 17.80  ? 182 GLY A O   1 
ATOM   1550 N  N   . LEU A 1 183 ? 11.938  -2.226  4.767   1.00 14.50  ? 183 LEU A N   1 
ATOM   1551 C  CA  . LEU A 1 183 ? 10.802  -2.965  4.228   1.00 13.16  ? 183 LEU A CA  1 
ATOM   1552 C  C   . LEU A 1 183 ? 10.969  -3.207  2.745   1.00 11.69  ? 183 LEU A C   1 
ATOM   1553 O  O   . LEU A 1 183 ? 10.083  -3.836  2.176   1.00 12.82  ? 183 LEU A O   1 
ATOM   1554 C  CB  . LEU A 1 183 ? 9.564   -2.145  4.496   1.00 15.49  ? 183 LEU A CB  1 
ATOM   1555 C  CG  . LEU A 1 183 ? 9.127   -2.071  5.965   1.00 15.91  ? 183 LEU A CG  1 
ATOM   1556 C  CD1 . LEU A 1 183 ? 7.925   -1.210  6.139   1.00 19.04  ? 183 LEU A CD1 1 
ATOM   1557 C  CD2 . LEU A 1 183 ? 9.055   -3.361  6.720   1.00 20.55  ? 183 LEU A CD2 1 
ATOM   1558 N  N   . LEU A 1 184 ? 12.037  -2.708  2.126   1.00 13.91  ? 184 LEU A N   1 
ATOM   1559 C  CA  . LEU A 1 184 ? 12.196  -2.739  0.673   1.00 12.47  ? 184 LEU A CA  1 
ATOM   1560 C  C   . LEU A 1 184 ? 12.903  -4.014  0.240   1.00 15.67  ? 184 LEU A C   1 
ATOM   1561 O  O   . LEU A 1 184 ? 13.811  -4.462  0.931   1.00 34.15  ? 184 LEU A O   1 
ATOM   1562 C  CB  . LEU A 1 184 ? 12.948  -1.478  0.143   1.00 11.97  ? 184 LEU A CB  1 
ATOM   1563 C  CG  . LEU A 1 184 ? 12.465  -0.112  0.529   1.00 11.75  ? 184 LEU A CG  1 
ATOM   1564 C  CD1 . LEU A 1 184 ? 13.293  1.044   -0.006  1.00 11.35  ? 184 LEU A CD1 1 
ATOM   1565 C  CD2 . LEU A 1 184 ? 11.040  0.065   0.029   1.00 12.81  ? 184 LEU A CD2 1 
ATOM   1566 N  N   . PRO A 1 185 ? 12.585  -4.569  -0.934  1.00 13.63  ? 185 PRO A N   1 
ATOM   1567 C  CA  . PRO A 1 185 ? 13.328  -5.689  -1.488  1.00 14.57  ? 185 PRO A CA  1 
ATOM   1568 C  C   . PRO A 1 185 ? 14.615  -5.120  -2.161  1.00 13.56  ? 185 PRO A C   1 
ATOM   1569 O  O   . PRO A 1 185 ? 14.836  -3.908  -2.252  1.00 24.31  ? 185 PRO A O   1 
ATOM   1570 C  CB  . PRO A 1 185 ? 12.360  -6.253  -2.549  1.00 13.85  ? 185 PRO A CB  1 
ATOM   1571 C  CG  . PRO A 1 185 ? 11.703  -4.998  -3.071  1.00 12.45  ? 185 PRO A CG  1 
ATOM   1572 C  CD  . PRO A 1 185 ? 11.472  -4.162  -1.809  1.00 9.41   ? 185 PRO A CD  1 
ATOM   1573 N  N   . GLU A 1 186 ? 15.456  -6.031  -2.661  1.00 13.28  ? 186 GLU A N   1 
ATOM   1574 C  CA  . GLU A 1 186 ? 16.708  -5.636  -3.274  1.00 18.79  ? 186 GLU A CA  1 
ATOM   1575 C  C   . GLU A 1 186 ? 16.499  -4.833  -4.527  1.00 15.86  ? 186 GLU A C   1 
ATOM   1576 O  O   . GLU A 1 186 ? 17.108  -3.754  -4.681  1.00 20.40  ? 186 GLU A O   1 
ATOM   1577 C  CB  . GLU A 1 186 ? 17.534  -6.841  -3.678  1.00 22.53  ? 186 GLU A CB  1 
ATOM   1578 C  CG  . GLU A 1 186 ? 18.235  -7.472  -2.526  1.00 27.44  ? 186 GLU A CG  1 
ATOM   1579 C  CD  . GLU A 1 186 ? 19.048  -8.692  -2.959  1.00 26.55  ? 186 GLU A CD  1 
ATOM   1580 O  OE1 . GLU A 1 186 ? 19.615  -9.382  -2.062  1.00 35.81  ? 186 GLU A OE1 1 
ATOM   1581 O  OE2 . GLU A 1 186 ? 19.148  -8.904  -4.188  1.00 25.15  ? 186 GLU A OE2 1 
ATOM   1582 N  N   . SER A 1 187 ? 15.640  -5.341  -5.409  1.00 17.62  ? 187 SER A N   1 
ATOM   1583 C  CA  . SER A 1 187 ? 15.449  -4.746  -6.697  1.00 16.28  ? 187 SER A CA  1 
ATOM   1584 C  C   . SER A 1 187 ? 14.342  -3.669  -6.619  1.00 13.31  ? 187 SER A C   1 
ATOM   1585 O  O   . SER A 1 187 ? 13.263  -3.915  -6.018  1.00 14.75  ? 187 SER A O   1 
ATOM   1586 C  CB  . SER A 1 187 ? 15.078  -5.793  -7.739  1.00 16.06  ? 187 SER A CB  1 
ATOM   1587 O  OG  . SER A 1 187 ? 14.844  -5.200  -8.997  1.00 17.60  ? 187 SER A OG  1 
ATOM   1588 N  N   . LEU A 1 188 ? 14.468  -2.613  -7.425  1.00 15.79  ? 188 LEU A N   1 
ATOM   1589 C  CA  . LEU A 1 188 ? 13.408  -1.603  -7.640  1.00 13.15  ? 188 LEU A CA  1 
ATOM   1590 C  C   . LEU A 1 188 ? 12.739  -1.778  -9.010  1.00 13.11  ? 188 LEU A C   1 
ATOM   1591 O  O   . LEU A 1 188 ? 12.081  -0.867  -9.489  1.00 15.11  ? 188 LEU A O   1 
ATOM   1592 C  CB  . LEU A 1 188 ? 13.848  -0.148  -7.349  1.00 16.37  ? 188 LEU A CB  1 
ATOM   1593 C  CG  . LEU A 1 188 ? 14.321  0.249   -5.895  1.00 25.11  ? 188 LEU A CG  1 
ATOM   1594 C  CD1 . LEU A 1 188 ? 14.841  1.728   -5.846  1.00 25.10  ? 188 LEU A CD1 1 
ATOM   1595 C  CD2 . LEU A 1 188 ? 13.139  -0.018  -4.939  1.00 24.65  ? 188 LEU A CD2 1 
ATOM   1596 N  N   . ASP A 1 189 ? 12.920  -2.915  -9.652  1.00 14.06  ? 189 ASP A N   1 
ATOM   1597 C  CA  . ASP A 1 189 ? 12.182  -3.135  -10.873 1.00 12.88  ? 189 ASP A CA  1 
ATOM   1598 C  C   . ASP A 1 189 ? 10.656  -3.113  -10.562 1.00 9.25   ? 189 ASP A C   1 
ATOM   1599 O  O   . ASP A 1 189 ? 10.236  -3.631  -9.540  1.00 9.56   ? 189 ASP A O   1 
ATOM   1600 C  CB  . ASP A 1 189 ? 12.506  -4.497  -11.471 1.00 14.34  ? 189 ASP A CB  1 
ATOM   1601 C  CG  . ASP A 1 189 ? 13.894  -4.611  -12.118 1.00 25.51  ? 189 ASP A CG  1 
ATOM   1602 O  OD1 . ASP A 1 189 ? 14.583  -3.593  -12.282 1.00 41.42  ? 189 ASP A OD1 1 
ATOM   1603 O  OD2 . ASP A 1 189 ? 14.242  -5.752  -12.338 1.00 36.00  ? 189 ASP A OD2 1 
ATOM   1604 N  N   . TYR A 1 190 ? 9.903   -2.512  -11.472 1.00 9.54   ? 190 TYR A N   1 
ATOM   1605 C  CA  . TYR A 1 190 ? 8.474   -2.272  -11.162 1.00 8.20   ? 190 TYR A CA  1 
ATOM   1606 C  C   . TYR A 1 190 ? 7.605   -2.332  -12.382 1.00 7.83   ? 190 TYR A C   1 
ATOM   1607 O  O   . TYR A 1 190 ? 8.023   -2.195  -13.523 1.00 9.10   ? 190 TYR A O   1 
ATOM   1608 C  CB  . TYR A 1 190 ? 8.306   -0.898  -10.483 1.00 9.68   ? 190 TYR A CB  1 
ATOM   1609 C  CG  . TYR A 1 190 ? 8.713   0.301   -11.321 1.00 9.03   ? 190 TYR A CG  1 
ATOM   1610 C  CD1 . TYR A 1 190 ? 7.792   0.932   -12.155 1.00 9.24   ? 190 TYR A CD1 1 
ATOM   1611 C  CD2 . TYR A 1 190 ? 10.012  0.831   -11.260 1.00 9.37   ? 190 TYR A CD2 1 
ATOM   1612 C  CE1 . TYR A 1 190 ? 8.142   1.999   -12.994 1.00 9.18   ? 190 TYR A CE1 1 
ATOM   1613 C  CE2 . TYR A 1 190 ? 10.343  1.888   -12.090 1.00 10.19  ? 190 TYR A CE2 1 
ATOM   1614 C  CZ  . TYR A 1 190 ? 9.437   2.505   -12.923 1.00 9.23   ? 190 TYR A CZ  1 
ATOM   1615 O  OH  . TYR A 1 190 ? 9.770   3.533   -13.741 1.00 12.47  ? 190 TYR A OH  1 
ATOM   1616 N  N   . TRP A 1 191 ? 6.269   -2.462  -12.069 1.00 7.18   ? 191 TRP A N   1 
ATOM   1617 C  CA  . TRP A 1 191 ? 5.182   -2.216  -13.035 1.00 7.10   ? 191 TRP A CA  1 
ATOM   1618 C  C   . TRP A 1 191 ? 4.518   -0.909  -12.629 1.00 6.75   ? 191 TRP A C   1 
ATOM   1619 O  O   . TRP A 1 191 ? 4.448   -0.606  -11.473 1.00 7.48   ? 191 TRP A O   1 
ATOM   1620 C  CB  . TRP A 1 191 ? 4.144   -3.317  -13.080 1.00 7.95   ? 191 TRP A CB  1 
ATOM   1621 C  CG  . TRP A 1 191 ? 4.682   -4.675  -13.501 1.00 9.16   ? 191 TRP A CG  1 
ATOM   1622 C  CD1 . TRP A 1 191 ? 4.928   -5.116  -14.795 1.00 10.30  ? 191 TRP A CD1 1 
ATOM   1623 C  CD2 . TRP A 1 191 ? 4.974   -5.790  -12.652 1.00 9.34   ? 191 TRP A CD2 1 
ATOM   1624 N  NE1 . TRP A 1 191 ? 5.305   -6.434  -14.770 1.00 10.72  ? 191 TRP A NE1 1 
ATOM   1625 C  CE2 . TRP A 1 191 ? 5.382   -6.869  -13.487 1.00 10.03  ? 191 TRP A CE2 1 
ATOM   1626 C  CE3 . TRP A 1 191 ? 4.859   -6.031  -11.268 1.00 10.71  ? 191 TRP A CE3 1 
ATOM   1627 C  CZ2 . TRP A 1 191 ? 5.675   -8.119  -12.943 1.00 10.28  ? 191 TRP A CZ2 1 
ATOM   1628 C  CZ3 . TRP A 1 191 ? 5.128   -7.277  -10.748 1.00 12.24  ? 191 TRP A CZ3 1 
ATOM   1629 C  CH2 . TRP A 1 191 ? 5.500   -8.330  -11.579 1.00 11.58  ? 191 TRP A CH2 1 
ATOM   1630 N  N   . THR A 1 192 ? 3.965   -0.197  -13.589 1.00 6.40   ? 192 THR A N   1 
ATOM   1631 C  CA  . THR A 1 192 ? 3.217   1.008   -13.230 1.00 6.82   ? 192 THR A CA  1 
ATOM   1632 C  C   . THR A 1 192 ? 1.998   1.211   -14.138 1.00 6.81   ? 192 THR A C   1 
ATOM   1633 O  O   . THR A 1 192 ? 1.968   0.832   -15.301 1.00 7.70   ? 192 THR A O   1 
ATOM   1634 C  CB  . THR A 1 192 ? 4.141   2.248   -13.369 1.00 7.31   ? 192 THR A CB  1 
ATOM   1635 O  OG1 . THR A 1 192 ? 3.469   3.435   -12.988 1.00 7.45   ? 192 THR A OG1 1 
ATOM   1636 C  CG2 . THR A 1 192 ? 4.717   2.444   -14.765 1.00 8.60   ? 192 THR A CG2 1 
ATOM   1637 N  N   . TYR A 1 193 ? 0.913   1.772   -13.547 1.00 6.75   ? 193 TYR A N   1 
ATOM   1638 C  CA  . TYR A 1 193 ? -0.284  2.052   -14.322 1.00 7.66   ? 193 TYR A CA  1 
ATOM   1639 C  C   . TYR A 1 193 ? -1.043  3.111   -13.530 1.00 7.04   ? 193 TYR A C   1 
ATOM   1640 O  O   . TYR A 1 193 ? -0.849  3.304   -12.334 1.00 7.52   ? 193 TYR A O   1 
ATOM   1641 C  CB  . TYR A 1 193 ? -1.131  0.766   -14.518 1.00 7.07   ? 193 TYR A CB  1 
ATOM   1642 C  CG  . TYR A 1 193 ? -1.789  0.327   -13.236 1.00 7.19   ? 193 TYR A CG  1 
ATOM   1643 C  CD1 . TYR A 1 193 ? -1.133  -0.409  -12.260 1.00 6.59   ? 193 TYR A CD1 1 
ATOM   1644 C  CD2 . TYR A 1 193 ? -3.137  0.680   -12.970 1.00 6.51   ? 193 TYR A CD2 1 
ATOM   1645 C  CE1 . TYR A 1 193 ? -1.749  -0.748  -11.059 1.00 7.16   ? 193 TYR A CE1 1 
ATOM   1646 C  CE2 . TYR A 1 193 ? -3.767  0.312   -11.798 1.00 6.51   ? 193 TYR A CE2 1 
ATOM   1647 C  CZ  . TYR A 1 193 ? -3.100  -0.375  -10.828 1.00 5.91   ? 193 TYR A CZ  1 
ATOM   1648 O  OH  . TYR A 1 193 ? -3.706  -0.721  -9.662  1.00 6.23   ? 193 TYR A OH  1 
ATOM   1649 N  N   . PRO A 1 194 ? -2.005  3.789   -14.190 1.00 7.19   ? 194 PRO A N   1 
ATOM   1650 C  CA  . PRO A 1 194 ? -2.806  4.827   -13.511 1.00 8.20   ? 194 PRO A CA  1 
ATOM   1651 C  C   . PRO A 1 194 ? -4.036  4.149   -12.847 1.00 7.28   ? 194 PRO A C   1 
ATOM   1652 O  O   . PRO A 1 194 ? -4.804  3.342   -13.523 1.00 8.40   ? 194 PRO A O   1 
ATOM   1653 C  CB  . PRO A 1 194 ? -3.316  5.686   -14.680 1.00 8.64   ? 194 PRO A CB  1 
ATOM   1654 C  CG  . PRO A 1 194 ? -3.245  4.763   -15.895 1.00 8.98   ? 194 PRO A CG  1 
ATOM   1655 C  CD  . PRO A 1 194 ? -2.141  3.781   -15.616 1.00 8.22   ? 194 PRO A CD  1 
ATOM   1656 N  N   . GLY A 1 195 ? -4.278  4.441   -11.585 1.00 6.83   ? 195 GLY A N   1 
ATOM   1657 C  CA  . GLY A 1 195 ? -5.426  3.828   -10.884 1.00 8.41   ? 195 GLY A CA  1 
ATOM   1658 C  C   . GLY A 1 195 ? -5.934  4.718   -9.793  1.00 7.32   ? 195 GLY A C   1 
ATOM   1659 O  O   . GLY A 1 195 ? -6.068  5.923   -9.926  1.00 7.24   ? 195 GLY A O   1 
ATOM   1660 N  N   . SER A 1 196 ? -6.329  4.033   -8.719  1.00 6.35   ? 196 SER A N   1 
ATOM   1661 C  CA  . SER A 1 196 ? -7.139  4.670   -7.682  1.00 7.30   ? 196 SER A CA  1 
ATOM   1662 C  C   . SER A 1 196 ? -6.720  4.233   -6.292  1.00 7.10   ? 196 SER A C   1 
ATOM   1663 O  O   . SER A 1 196 ? -5.998  3.255   -6.115  1.00 6.54   ? 196 SER A O   1 
ATOM   1664 C  CB  . SER A 1 196 ? -8.659  4.288   -7.885  1.00 7.41   ? 196 SER A CB  1 
ATOM   1665 O  OG  . SER A 1 196 ? -8.866  2.929   -7.477  1.00 7.69   ? 196 SER A OG  1 
ATOM   1666 N  N   . LEU A 1 197 ? -7.303  4.905   -5.277  1.00 7.80   ? 197 LEU A N   1 
ATOM   1667 C  CA  . LEU A 1 197 ? -7.287  4.318   -3.949  1.00 7.05   ? 197 LEU A CA  1 
ATOM   1668 C  C   . LEU A 1 197 ? -7.998  2.964   -3.978  1.00 7.18   ? 197 LEU A C   1 
ATOM   1669 O  O   . LEU A 1 197 ? -8.974  2.786   -4.792  1.00 7.26   ? 197 LEU A O   1 
ATOM   1670 C  CB  . LEU A 1 197 ? -8.016  5.214   -2.943  1.00 8.24   ? 197 LEU A CB  1 
ATOM   1671 C  CG  . LEU A 1 197 ? -7.556  6.675   -2.852  1.00 7.80   ? 197 LEU A CG  1 
ATOM   1672 C  CD1 . LEU A 1 197 ? -8.409  7.339   -1.734  1.00 9.38   ? 197 LEU A CD1 1 
ATOM   1673 C  CD2 . LEU A 1 197 ? -6.038  6.748   -2.506  1.00 11.79  ? 197 LEU A CD2 1 
ATOM   1674 N  N   . THR A 1 198 ? -7.613  2.058   -3.126  1.00 7.25   ? 198 THR A N   1 
ATOM   1675 C  CA  . THR A 1 198 ? -8.329  0.763   -3.051  1.00 7.39   ? 198 THR A CA  1 
ATOM   1676 C  C   . THR A 1 198 ? -9.324  0.730   -1.886  1.00 6.85   ? 198 THR A C   1 
ATOM   1677 O  O   . THR A 1 198 ? -9.881  -0.374  -1.707  1.00 7.75   ? 198 THR A O   1 
ATOM   1678 C  CB  . THR A 1 198 ? -7.328  -0.404  -2.985  1.00 6.84   ? 198 THR A CB  1 
ATOM   1679 O  OG1 . THR A 1 198 ? -6.745  -0.401  -1.701  1.00 6.20   ? 198 THR A OG1 1 
ATOM   1680 C  CG2 . THR A 1 198 ? -6.300  -0.438  -4.099  1.00 7.49   ? 198 THR A CG2 1 
ATOM   1681 N  N   . THR A 1 199 ? -9.497  1.822   -1.195  1.00 8.20   ? 199 THR A N   1 
ATOM   1682 C  CA  . THR A 1 199 ? -10.501 1.908   -0.151  1.00 8.04   ? 199 THR A CA  1 
ATOM   1683 C  C   . THR A 1 199 ? -11.293 3.148   -0.469  1.00 8.17   ? 199 THR A C   1 
ATOM   1684 O  O   . THR A 1 199 ? -10.872 4.064   -1.147  1.00 8.22   ? 199 THR A O   1 
ATOM   1685 C  CB  . THR A 1 199 ? -9.929  2.105   1.259   1.00 10.87  ? 199 THR A CB  1 
ATOM   1686 O  OG1 . THR A 1 199 ? -8.970  3.198   1.259   1.00 14.30  ? 199 THR A OG1 1 
ATOM   1687 C  CG2 . THR A 1 199 ? -9.135  0.876   1.634   1.00 9.63   ? 199 THR A CG2 1 
ATOM   1688 N  N   . PRO A 1 200 ? -12.574 3.197   -0.016  1.00 9.04   ? 200 PRO A N   1 
ATOM   1689 C  CA  . PRO A 1 200 ? -13.373 4.424   -0.101  1.00 9.99   ? 200 PRO A CA  1 
ATOM   1690 C  C   . PRO A 1 200 ? -12.536 5.600   0.370   1.00 8.90   ? 200 PRO A C   1 
ATOM   1691 O  O   . PRO A 1 200 ? -11.786 5.496   1.391   1.00 11.20  ? 200 PRO A O   1 
ATOM   1692 C  CB  . PRO A 1 200 ? -14.544 4.104   0.862   1.00 14.86  ? 200 PRO A CB  1 
ATOM   1693 C  CG  . PRO A 1 200 ? -14.810 2.628   0.566   1.00 11.79  ? 200 PRO A CG  1 
ATOM   1694 C  CD  . PRO A 1 200 ? -13.358 2.086   0.600   1.00 12.41  ? 200 PRO A CD  1 
ATOM   1695 N  N   . PRO A 1 201 ? -12.591 6.723   -0.336  1.00 9.16   ? 201 PRO A N   1 
ATOM   1696 C  CA  . PRO A 1 201 ? -13.501 7.047   -1.410  1.00 10.28  ? 201 PRO A CA  1 
ATOM   1697 C  C   . PRO A 1 201 ? -13.130 6.591   -2.828  1.00 8.84   ? 201 PRO A C   1 
ATOM   1698 O  O   . PRO A 1 201 ? -13.798 6.950   -3.793  1.00 9.05   ? 201 PRO A O   1 
ATOM   1699 C  CB  . PRO A 1 201 ? -13.536 8.577   -1.367  1.00 11.56  ? 201 PRO A CB  1 
ATOM   1700 C  CG  . PRO A 1 201 ? -12.141 8.896   -0.987  1.00 11.89  ? 201 PRO A CG  1 
ATOM   1701 C  CD  . PRO A 1 201 ? -11.776 7.868   0.063   1.00 12.06  ? 201 PRO A CD  1 
ATOM   1702 N  N   . LEU A 1 202 ? -12.081 5.736   -2.973  1.00 8.52   ? 202 LEU A N   1 
ATOM   1703 C  CA  . LEU A 1 202 ? -11.774 5.125   -4.252  1.00 7.59   ? 202 LEU A CA  1 
ATOM   1704 C  C   . LEU A 1 202 ? -11.416 6.144   -5.341  1.00 8.44   ? 202 LEU A C   1 
ATOM   1705 O  O   . LEU A 1 202 ? -11.550 5.925   -6.519  1.00 9.43   ? 202 LEU A O   1 
ATOM   1706 C  CB  . LEU A 1 202 ? -12.962 4.212   -4.721  1.00 8.22   ? 202 LEU A CB  1 
ATOM   1707 C  CG  . LEU A 1 202 ? -13.270 3.072   -3.752  1.00 9.22   ? 202 LEU A CG  1 
ATOM   1708 C  CD1 . LEU A 1 202 ? -14.614 2.413   -4.151  1.00 12.54  ? 202 LEU A CD1 1 
ATOM   1709 C  CD2 . LEU A 1 202 ? -12.161 2.047   -3.641  1.00 8.89   ? 202 LEU A CD2 1 
ATOM   1710 N  N   . ALA A 1 203 ? -10.884 7.288   -4.863  1.00 8.14   ? 203 ALA A N   1 
ATOM   1711 C  CA  . ALA A 1 203 ? -10.542 8.405   -5.754  1.00 7.78   ? 203 ALA A CA  1 
ATOM   1712 C  C   . ALA A 1 203 ? -9.510  7.965   -6.802  1.00 7.81   ? 203 ALA A C   1 
ATOM   1713 O  O   . ALA A 1 203 ? -8.531  7.227   -6.502  1.00 7.42   ? 203 ALA A O   1 
ATOM   1714 C  CB  . ALA A 1 203 ? -9.956  9.548   -4.943  1.00 8.59   ? 203 ALA A CB  1 
ATOM   1715 N  N   . GLU A 1 204 ? -9.712  8.447   -8.014  1.00 8.38   ? 204 GLU A N   1 
ATOM   1716 C  CA  . GLU A 1 204 ? -8.887  8.061   -9.178  1.00 7.79   ? 204 GLU A CA  1 
ATOM   1717 C  C   . GLU A 1 204 ? -7.709  9.044   -9.360  1.00 7.98   ? 204 GLU A C   1 
ATOM   1718 O  O   . GLU A 1 204 ? -7.630  9.810   -10.290 1.00 9.54   ? 204 GLU A O   1 
ATOM   1719 C  CB  . GLU A 1 204 ? -9.774  7.983   -10.434 1.00 9.55   ? 204 GLU A CB  1 
ATOM   1720 C  CG  . GLU A 1 204 ? -10.699 6.734   -10.266 1.00 11.74  ? 204 GLU A CG  1 
ATOM   1721 C  CD  . GLU A 1 204 ? -11.577 6.425   -11.472 1.00 10.99  ? 204 GLU A CD  1 
ATOM   1722 O  OE1 . GLU A 1 204 ? -11.883 7.372   -12.183 1.00 13.59  ? 204 GLU A OE1 1 
ATOM   1723 O  OE2 . GLU A 1 204 ? -11.898 5.236   -11.645 1.00 10.05  ? 204 GLU A OE2 1 
ATOM   1724 N  N   . CYS A 1 205 ? -6.868  8.958   -8.350  1.00 7.60   ? 205 CYS A N   1 
ATOM   1725 C  CA  . CYS A 1 205 ? -5.797  9.972   -8.160  1.00 8.05   ? 205 CYS A CA  1 
ATOM   1726 C  C   . CYS A 1 205 ? -4.386  9.371   -8.049  1.00 7.93   ? 205 CYS A C   1 
ATOM   1727 O  O   . CYS A 1 205 ? -3.437  10.081  -7.632  1.00 8.50   ? 205 CYS A O   1 
ATOM   1728 C  CB  . CYS A 1 205 ? -6.070  10.823  -6.925  1.00 8.58   ? 205 CYS A CB  1 
ATOM   1729 S  SG  . CYS A 1 205 ? -6.126  9.878   -5.380  1.00 8.11   ? 205 CYS A SG  1 
ATOM   1730 N  N   . VAL A 1 206 ? -4.236  8.085   -8.304  1.00 6.94   ? 206 VAL A N   1 
ATOM   1731 C  CA  . VAL A 1 206 ? -3.013  7.365   -7.945  1.00 6.54   ? 206 VAL A CA  1 
ATOM   1732 C  C   . VAL A 1 206 ? -2.278  6.932   -9.185  1.00 5.94   ? 206 VAL A C   1 
ATOM   1733 O  O   . VAL A 1 206 ? -2.778  6.236   -10.069 1.00 7.30   ? 206 VAL A O   1 
ATOM   1734 C  CB  . VAL A 1 206 ? -3.316  6.112   -7.076  1.00 6.75   ? 206 VAL A CB  1 
ATOM   1735 C  CG1 . VAL A 1 206 ? -1.953  5.355   -6.769  1.00 8.65   ? 206 VAL A CG1 1 
ATOM   1736 C  CG2 . VAL A 1 206 ? -4.090  6.501   -5.826  1.00 7.27   ? 206 VAL A CG2 1 
ATOM   1737 N  N   . THR A 1 207 ? -0.919  7.223   -9.201  1.00 6.38   ? 207 THR A N   1 
ATOM   1738 C  CA  . THR A 1 207 ? -0.008  6.473   -10.032 1.00 6.66   ? 207 THR A CA  1 
ATOM   1739 C  C   . THR A 1 207 ? 0.527   5.323   -9.197  1.00 5.93   ? 207 THR A C   1 
ATOM   1740 O  O   . THR A 1 207 ? 1.174   5.499   -8.156  1.00 6.14   ? 207 THR A O   1 
ATOM   1741 C  CB  . THR A 1 207 ? 1.205   7.327   -10.474 1.00 8.23   ? 207 THR A CB  1 
ATOM   1742 O  OG1 . THR A 1 207 ? 0.711   8.490   -11.183 1.00 8.95   ? 207 THR A OG1 1 
ATOM   1743 C  CG2 . THR A 1 207 ? 2.122   6.510   -11.396 1.00 9.15   ? 207 THR A CG2 1 
ATOM   1744 N  N   . TRP A 1 208 ? 0.193   4.071   -9.670  1.00 6.57   ? 208 TRP A N   1 
ATOM   1745 C  CA  . TRP A 1 208 ? 0.649   2.918   -8.957  1.00 7.09   ? 208 TRP A CA  1 
ATOM   1746 C  C   . TRP A 1 208 ? 2.048   2.529   -9.470  1.00 6.29   ? 208 TRP A C   1 
ATOM   1747 O  O   . TRP A 1 208 ? 2.265   2.444   -10.663 1.00 7.57   ? 208 TRP A O   1 
ATOM   1748 C  CB  . TRP A 1 208 ? -0.351  1.748   -9.210  1.00 6.66   ? 208 TRP A CB  1 
ATOM   1749 C  CG  . TRP A 1 208 ? -1.504  1.801   -8.218  1.00 6.49   ? 208 TRP A CG  1 
ATOM   1750 C  CD1 . TRP A 1 208 ? -2.744  2.411   -8.415  1.00 6.04   ? 208 TRP A CD1 1 
ATOM   1751 C  CD2 . TRP A 1 208 ? -1.428  1.411   -6.867  1.00 6.58   ? 208 TRP A CD2 1 
ATOM   1752 N  NE1 . TRP A 1 208 ? -3.401  2.395   -7.252  1.00 6.16   ? 208 TRP A NE1 1 
ATOM   1753 C  CE2 . TRP A 1 208 ? -2.669  1.776   -6.274  1.00 6.54   ? 208 TRP A CE2 1 
ATOM   1754 C  CE3 . TRP A 1 208 ? -0.490  0.748   -6.065  1.00 6.79   ? 208 TRP A CE3 1 
ATOM   1755 C  CZ2 . TRP A 1 208 ? -2.966  1.524   -4.965  1.00 7.62   ? 208 TRP A CZ2 1 
ATOM   1756 C  CZ3 . TRP A 1 208 ? -0.786  0.460   -4.782  1.00 7.01   ? 208 TRP A CZ3 1 
ATOM   1757 C  CH2 . TRP A 1 208 ? -2.060  0.792   -4.224  1.00 7.11   ? 208 TRP A CH2 1 
ATOM   1758 N  N   . ILE A 1 209 ? 2.871   2.095   -8.501  1.00 6.20   ? 209 ILE A N   1 
ATOM   1759 C  CA  . ILE A 1 209 ? 4.238   1.581   -8.816  1.00 6.92   ? 209 ILE A CA  1 
ATOM   1760 C  C   . ILE A 1 209 ? 4.347   0.335   -7.983  1.00 7.20   ? 209 ILE A C   1 
ATOM   1761 O  O   . ILE A 1 209 ? 4.406   0.419   -6.785  1.00 7.43   ? 209 ILE A O   1 
ATOM   1762 C  CB  . ILE A 1 209 ? 5.317   2.603   -8.420  1.00 8.51   ? 209 ILE A CB  1 
ATOM   1763 C  CG1 . ILE A 1 209 ? 5.130   3.861   -9.257  1.00 10.77  ? 209 ILE A CG1 1 
ATOM   1764 C  CG2 . ILE A 1 209 ? 6.757   1.978   -8.666  1.00 13.21  ? 209 ILE A CG2 1 
ATOM   1765 C  CD1 . ILE A 1 209 ? 5.899   5.157   -8.774  1.00 13.49  ? 209 ILE A CD1 1 
ATOM   1766 N  N   . VAL A 1 210 ? 4.284   -0.831  -8.669  1.00 7.72   ? 210 VAL A N   1 
ATOM   1767 C  CA  . VAL A 1 210 ? 4.272   -2.105  -7.961  1.00 6.53   ? 210 VAL A CA  1 
ATOM   1768 C  C   . VAL A 1 210 ? 5.600   -2.825  -8.186  1.00 6.28   ? 210 VAL A C   1 
ATOM   1769 O  O   . VAL A 1 210 ? 5.918   -3.114  -9.329  1.00 7.02   ? 210 VAL A O   1 
ATOM   1770 C  CB  . VAL A 1 210 ? 3.059   -2.958  -8.439  1.00 7.83   ? 210 VAL A CB  1 
ATOM   1771 C  CG1 . VAL A 1 210 ? 3.075   -4.288  -7.719  1.00 7.72   ? 210 VAL A CG1 1 
ATOM   1772 C  CG2 . VAL A 1 210 ? 1.719   -2.191  -8.102  1.00 9.52   ? 210 VAL A CG2 1 
ATOM   1773 N  N   . LEU A 1 211 ? 6.285   -3.125  -7.081  1.00 7.05   ? 211 LEU A N   1 
ATOM   1774 C  CA  . LEU A 1 211 ? 7.635   -3.724  -7.300  1.00 7.63   ? 211 LEU A CA  1 
ATOM   1775 C  C   . LEU A 1 211 ? 7.405   -5.189  -7.679  1.00 7.53   ? 211 LEU A C   1 
ATOM   1776 O  O   . LEU A 1 211 ? 6.593   -5.935  -7.126  1.00 7.52   ? 211 LEU A O   1 
ATOM   1777 C  CB  . LEU A 1 211 ? 8.415   -3.616  -5.992  1.00 8.09   ? 211 LEU A CB  1 
ATOM   1778 C  CG  . LEU A 1 211 ? 8.811   -2.188  -5.621  1.00 9.01   ? 211 LEU A CG  1 
ATOM   1779 C  CD1 . LEU A 1 211 ? 9.823   -2.196  -4.456  1.00 11.83  ? 211 LEU A CD1 1 
ATOM   1780 C  CD2 . LEU A 1 211 ? 9.374   -1.325  -6.764  1.00 10.18  ? 211 LEU A CD2 1 
ATOM   1781 N  N   . LYS A 1 212 ? 8.271   -5.673  -8.598  1.00 7.86   ? 212 LYS A N   1 
ATOM   1782 C  CA  . LYS A 1 212 ? 8.263   -7.056  -8.986  1.00 8.78   ? 212 LYS A CA  1 
ATOM   1783 C  C   . LYS A 1 212 ? 8.730   -8.029  -7.941  1.00 7.39   ? 212 LYS A C   1 
ATOM   1784 O  O   . LYS A 1 212 ? 8.228   -9.149  -7.832  1.00 9.31   ? 212 LYS A O   1 
ATOM   1785 C  CB  . LYS A 1 212 ? 8.936   -7.308  -10.317 1.00 10.28  ? 212 LYS A CB  1 
ATOM   1786 C  CG  . LYS A 1 212 ? 9.102   -8.792  -10.705 1.00 15.99  ? 212 LYS A CG  1 
ATOM   1787 C  CD  . LYS A 1 212 ? 9.655   -9.129  -12.082 1.00 19.62  ? 212 LYS A CD  1 
ATOM   1788 C  CE  . LYS A 1 212 ? 9.827   -10.612 -12.330 1.00 23.14  ? 212 LYS A CE  1 
ATOM   1789 N  NZ  . LYS A 1 212 ? 10.688  -10.915 -13.504 1.00 35.25  ? 212 LYS A NZ  1 
ATOM   1790 N  N   . GLU A 1 213 ? 9.766   -7.633  -7.194  1.00 8.06   ? 213 GLU A N   1 
ATOM   1791 C  CA  . GLU A 1 213 ? 10.339  -8.526  -6.199  1.00 8.61   ? 213 GLU A CA  1 
ATOM   1792 C  C   . GLU A 1 213 ? 9.559   -8.457  -4.892  1.00 7.46   ? 213 GLU A C   1 
ATOM   1793 O  O   . GLU A 1 213 ? 9.527   -7.407  -4.299  1.00 7.85   ? 213 GLU A O   1 
ATOM   1794 C  CB  . GLU A 1 213 ? 11.822  -8.170  -5.972  1.00 10.47  ? 213 GLU A CB  1 
ATOM   1795 C  CG  . GLU A 1 213 ? 12.520  -9.143  -5.016  1.00 11.92  ? 213 GLU A CG  1 
ATOM   1796 C  CD  . GLU A 1 213 ? 14.033  -8.845  -4.815  1.00 16.16  ? 213 GLU A CD  1 
ATOM   1797 O  OE1 . GLU A 1 213 ? 14.563  -7.964  -5.475  1.00 23.66  ? 213 GLU A OE1 1 
ATOM   1798 O  OE2 . GLU A 1 213 ? 14.647  -9.466  -3.944  1.00 33.72  ? 213 GLU A OE2 1 
ATOM   1799 N  N   . PRO A 1 214 ? 9.011   -9.605  -4.425  1.00 7.72   ? 214 PRO A N   1 
ATOM   1800 C  CA  . PRO A 1 214 ? 8.344   -9.564  -3.114  1.00 8.59   ? 214 PRO A CA  1 
ATOM   1801 C  C   . PRO A 1 214 ? 9.403   -9.527  -2.012  1.00 8.48   ? 214 PRO A C   1 
ATOM   1802 O  O   . PRO A 1 214 ? 10.574  -9.924  -2.224  1.00 10.57  ? 214 PRO A O   1 
ATOM   1803 C  CB  . PRO A 1 214 ? 7.620   -10.931 -3.033  1.00 8.30   ? 214 PRO A CB  1 
ATOM   1804 C  CG  . PRO A 1 214 ? 8.452   -11.840 -3.936  1.00 13.77  ? 214 PRO A CG  1 
ATOM   1805 C  CD  . PRO A 1 214 ? 8.933   -10.911 -5.067  1.00 9.16   ? 214 PRO A CD  1 
ATOM   1806 N  N   . ILE A 1 215 ? 9.008   -9.098  -0.823  1.00 8.50   ? 215 ILE A N   1 
ATOM   1807 C  CA  . ILE A 1 215 ? 9.806   -9.330  0.404   1.00 8.06   ? 215 ILE A CA  1 
ATOM   1808 C  C   . ILE A 1 215 ? 9.248   -10.604 1.062   1.00 8.70   ? 215 ILE A C   1 
ATOM   1809 O  O   . ILE A 1 215 ? 8.053   -10.964 0.897   1.00 9.08   ? 215 ILE A O   1 
ATOM   1810 C  CB  . ILE A 1 215 ? 9.701   -8.141  1.388   1.00 9.50   ? 215 ILE A CB  1 
ATOM   1811 C  CG1 . ILE A 1 215 ? 8.280   -7.809  1.865   1.00 9.71   ? 215 ILE A CG1 1 
ATOM   1812 C  CG2 . ILE A 1 215 ? 10.397  -6.916  0.727   1.00 10.42  ? 215 ILE A CG2 1 
ATOM   1813 C  CD1 . ILE A 1 215 ? 8.358   -6.874  3.105   1.00 13.05  ? 215 ILE A CD1 1 
ATOM   1814 N  N   A SER A 1 216 ? 10.138  -11.264 1.801   0.50 8.69   ? 216 SER A N   1 
ATOM   1815 N  N   B SER A 1 216 ? 10.106  -11.331 1.762   0.50 9.59   ? 216 SER A N   1 
ATOM   1816 C  CA  A SER A 1 216 ? 9.781   -12.384 2.659   0.50 8.03   ? 216 SER A CA  1 
ATOM   1817 C  CA  B SER A 1 216 ? 9.636   -12.461 2.544   0.50 10.62  ? 216 SER A CA  1 
ATOM   1818 C  C   A SER A 1 216 ? 9.461   -11.890 4.062   0.50 7.38   ? 216 SER A C   1 
ATOM   1819 C  C   B SER A 1 216 ? 9.526   -12.079 4.009   0.50 9.14   ? 216 SER A C   1 
ATOM   1820 O  O   A SER A 1 216 ? 10.186  -11.047 4.622   0.50 7.30   ? 216 SER A O   1 
ATOM   1821 O  O   B SER A 1 216 ? 10.464  -11.480 4.547   0.50 9.70   ? 216 SER A O   1 
ATOM   1822 C  CB  A SER A 1 216 ? 10.917  -13.450 2.623   0.50 10.47  ? 216 SER A CB  1 
ATOM   1823 C  CB  B SER A 1 216 ? 10.562  -13.637 2.311   0.50 13.95  ? 216 SER A CB  1 
ATOM   1824 O  OG  A SER A 1 216 ? 10.910  -14.138 1.349   0.50 13.63  ? 216 SER A OG  1 
ATOM   1825 O  OG  B SER A 1 216 ? 10.481  -14.595 3.328   0.50 14.93  ? 216 SER A OG  1 
ATOM   1826 N  N   . VAL A 1 217 ? 8.392   -12.451 4.628   1.00 8.31   ? 217 VAL A N   1 
ATOM   1827 C  CA  . VAL A 1 217 ? 8.095   -12.245 6.045   1.00 8.44   ? 217 VAL A CA  1 
ATOM   1828 C  C   . VAL A 1 217 ? 7.852   -13.633 6.642   1.00 7.86   ? 217 VAL A C   1 
ATOM   1829 O  O   . VAL A 1 217 ? 7.525   -14.587 5.952   1.00 9.05   ? 217 VAL A O   1 
ATOM   1830 C  CB  . VAL A 1 217 ? 6.914   -11.319 6.284   1.00 9.37   ? 217 VAL A CB  1 
ATOM   1831 C  CG1 . VAL A 1 217 ? 7.171   -9.954  5.609   1.00 9.71   ? 217 VAL A CG1 1 
ATOM   1832 C  CG2 . VAL A 1 217 ? 5.587   -11.975 5.790   1.00 10.22  ? 217 VAL A CG2 1 
ATOM   1833 N  N   . SER A 1 218 ? 8.028   -13.804 7.950   1.00 8.80   ? 218 SER A N   1 
ATOM   1834 C  CA  . SER A 1 218 ? 7.828   -15.133 8.516   1.00 9.71   ? 218 SER A CA  1 
ATOM   1835 C  C   . SER A 1 218 ? 6.353   -15.372 8.811   1.00 9.02   ? 218 SER A C   1 
ATOM   1836 O  O   . SER A 1 218 ? 5.551   -14.462 8.993   1.00 8.89   ? 218 SER A O   1 
ATOM   1837 C  CB  . SER A 1 218 ? 8.627   -15.321 9.796   1.00 11.11  ? 218 SER A CB  1 
ATOM   1838 O  OG  . SER A 1 218 ? 8.179   -14.430 10.785  1.00 12.32  ? 218 SER A OG  1 
ATOM   1839 N  N   A SER A 1 219 ? 6.082   -16.641 9.012   0.50 10.29  ? 219 SER A N   1 
ATOM   1840 N  N   B SER A 1 219 ? 6.001   -16.644 8.989   0.50 11.08  ? 219 SER A N   1 
ATOM   1841 C  CA  A SER A 1 219 ? 4.749   -17.034 9.415   0.50 11.12  ? 219 SER A CA  1 
ATOM   1842 C  CA  B SER A 1 219 ? 4.657   -16.995 9.461   0.50 12.00  ? 219 SER A CA  1 
ATOM   1843 C  C   A SER A 1 219 ? 4.404   -16.407 10.774  0.50 12.32  ? 219 SER A C   1 
ATOM   1844 C  C   B SER A 1 219 ? 4.378   -16.274 10.785  0.50 12.12  ? 219 SER A C   1 
ATOM   1845 O  O   A SER A 1 219 ? 3.287   -15.945 10.962  0.50 12.86  ? 219 SER A O   1 
ATOM   1846 O  O   B SER A 1 219 ? 3.280   -15.774 10.987  0.50 13.49  ? 219 SER A O   1 
ATOM   1847 C  CB  A SER A 1 219 ? 4.710   -18.524 9.384   0.50 10.51  ? 219 SER A CB  1 
ATOM   1848 C  CB  B SER A 1 219 ? 4.511   -18.505 9.598   0.50 15.27  ? 219 SER A CB  1 
ATOM   1849 O  OG  A SER A 1 219 ? 5.435   -19.084 10.455  0.50 10.62  ? 219 SER A OG  1 
ATOM   1850 O  OG  B SER A 1 219 ? 3.145   -18.901 9.634   0.50 17.50  ? 219 SER A OG  1 
ATOM   1851 N  N   A GLU A 1 220 ? 5.363   -16.293 11.708  0.50 12.33  ? 220 GLU A N   1 
ATOM   1852 N  N   B GLU A 1 220 ? 5.383   -16.168 11.673  0.50 12.77  ? 220 GLU A N   1 
ATOM   1853 C  CA  A GLU A 1 220 ? 5.051   -15.587 12.952  0.50 14.27  ? 220 GLU A CA  1 
ATOM   1854 C  CA  B GLU A 1 220 ? 5.189   -15.546 12.984  0.50 14.07  ? 220 GLU A CA  1 
ATOM   1855 C  C   A GLU A 1 220 ? 4.679   -14.112 12.716  0.50 12.43  ? 220 GLU A C   1 
ATOM   1856 C  C   B GLU A 1 220 ? 4.887   -14.046 12.876  0.50 9.94   ? 220 GLU A C   1 
ATOM   1857 O  O   A GLU A 1 220 ? 3.731   -13.624 13.322  0.50 14.27  ? 220 GLU A O   1 
ATOM   1858 O  O   B GLU A 1 220 ? 4.119   -13.509 13.659  0.50 13.86  ? 220 GLU A O   1 
ATOM   1859 C  CB  A GLU A 1 220 ? 6.154   -15.729 13.998  0.50 15.31  ? 220 GLU A CB  1 
ATOM   1860 C  CB  B GLU A 1 220 ? 6.406   -15.755 13.874  0.50 17.79  ? 220 GLU A CB  1 
ATOM   1861 C  CG  A GLU A 1 220 ? 6.475   -17.179 14.394  0.50 16.64  ? 220 GLU A CG  1 
ATOM   1862 C  CG  B GLU A 1 220 ? 6.872   -17.207 13.990  0.50 21.98  ? 220 GLU A CG  1 
ATOM   1863 C  CD  A GLU A 1 220 ? 7.497   -17.919 13.507  0.50 17.51  ? 220 GLU A CD  1 
ATOM   1864 C  CD  B GLU A 1 220 ? 7.705   -17.760 12.828  0.50 28.66  ? 220 GLU A CD  1 
ATOM   1865 O  OE1 A GLU A 1 220 ? 7.916   -17.355 12.467  0.50 12.70  ? 220 GLU A OE1 1 
ATOM   1866 O  OE1 B GLU A 1 220 ? 7.124   -18.102 11.790  0.50 25.74  ? 220 GLU A OE1 1 
ATOM   1867 O  OE2 A GLU A 1 220 ? 7.887   -19.046 13.865  0.50 20.12  ? 220 GLU A OE2 1 
ATOM   1868 O  OE2 B GLU A 1 220 ? 8.958   -17.845 12.953  0.50 38.16  ? 220 GLU A OE2 1 
ATOM   1869 N  N   . GLN A 1 221 ? 5.416   -13.403 11.846  1.00 10.56  ? 221 GLN A N   1 
ATOM   1870 C  CA  . GLN A 1 221 ? 5.159   -11.989 11.584  1.00 10.48  ? 221 GLN A CA  1 
ATOM   1871 C  C   . GLN A 1 221 ? 3.726   -11.788 11.074  1.00 10.14  ? 221 GLN A C   1 
ATOM   1872 O  O   . GLN A 1 221 ? 2.926   -10.975 11.583  1.00 11.46  ? 221 GLN A O   1 
ATOM   1873 C  CB  . GLN A 1 221 ? 6.246   -11.486 10.630  1.00 12.11  ? 221 GLN A CB  1 
ATOM   1874 C  CG  . GLN A 1 221 ? 7.608   -11.330 11.357  1.00 11.36  ? 221 GLN A CG  1 
ATOM   1875 C  CD  . GLN A 1 221 ? 8.644   -10.765 10.422  1.00 11.88  ? 221 GLN A CD  1 
ATOM   1876 O  OE1 . GLN A 1 221 ? 8.771   -11.132 9.243   1.00 11.64  ? 221 GLN A OE1 1 
ATOM   1877 N  NE2 . GLN A 1 221 ? 9.443   -9.898  11.032  1.00 12.16  ? 221 GLN A NE2 1 
ATOM   1878 N  N   A VAL A 1 222 ? 3.345   -12.607 10.089  0.50 10.41  ? 222 VAL A N   1 
ATOM   1879 N  N   B VAL A 1 222 ? 3.354   -12.619 10.084  0.50 11.07  ? 222 VAL A N   1 
ATOM   1880 C  CA  A VAL A 1 222 ? 2.015   -12.401 9.519   0.50 9.70   ? 222 VAL A CA  1 
ATOM   1881 C  CA  B VAL A 1 222 ? 2.008   -12.464 9.525   0.50 11.53  ? 222 VAL A CA  1 
ATOM   1882 C  C   A VAL A 1 222 ? 0.936   -12.857 10.521  0.50 11.82  ? 222 VAL A C   1 
ATOM   1883 C  C   B VAL A 1 222 ? 0.970   -12.817 10.576  0.50 11.23  ? 222 VAL A C   1 
ATOM   1884 O  O   A VAL A 1 222 ? -0.184  -12.300 10.580  0.50 11.40  ? 222 VAL A O   1 
ATOM   1885 O  O   B VAL A 1 222 ? -0.137  -12.253 10.589  0.50 11.63  ? 222 VAL A O   1 
ATOM   1886 C  CB  A VAL A 1 222 ? 1.916   -12.989 8.090   0.50 9.56   ? 222 VAL A CB  1 
ATOM   1887 C  CB  B VAL A 1 222 ? 1.751   -13.270 8.238   0.50 13.01  ? 222 VAL A CB  1 
ATOM   1888 C  CG1 A VAL A 1 222 ? 1.906   -14.514 8.101   0.50 8.48   ? 222 VAL A CG1 1 
ATOM   1889 C  CG1 B VAL A 1 222 ? 0.282   -13.156 7.824   0.50 15.05  ? 222 VAL A CG1 1 
ATOM   1890 C  CG2 A VAL A 1 222 ? 0.735   -12.399 7.340   0.50 9.90   ? 222 VAL A CG2 1 
ATOM   1891 C  CG2 B VAL A 1 222 ? 2.637   -12.704 7.158   0.50 11.30  ? 222 VAL A CG2 1 
ATOM   1892 N  N   . LEU A 1 223 ? 1.255   -13.832 11.382  1.00 12.47  ? 223 LEU A N   1 
ATOM   1893 C  CA  . LEU A 1 223 ? 0.292   -14.235 12.372  1.00 13.71  ? 223 LEU A CA  1 
ATOM   1894 C  C   . LEU A 1 223 ? 0.011   -13.091 13.326  1.00 12.25  ? 223 LEU A C   1 
ATOM   1895 O  O   . LEU A 1 223 ? -1.134  -12.945 13.761  1.00 13.42  ? 223 LEU A O   1 
ATOM   1896 C  CB  . LEU A 1 223 ? 0.732   -15.523 13.072  1.00 16.62  ? 223 LEU A CB  1 
ATOM   1897 C  CG  . LEU A 1 223 ? 0.523   -16.794 12.203  1.00 25.21  ? 223 LEU A CG  1 
ATOM   1898 C  CD1 . LEU A 1 223 ? 1.121   -18.022 12.892  1.00 25.41  ? 223 LEU A CD1 1 
ATOM   1899 C  CD2 . LEU A 1 223 ? -0.953  -17.047 11.878  1.00 29.47  ? 223 LEU A CD2 1 
ATOM   1900 N  N   . LYS A 1 224 ? 0.953   -12.210 13.583  1.00 12.93  ? 224 LYS A N   1 
ATOM   1901 C  CA  . LYS A 1 224 ? 0.720   -11.055 14.440  1.00 16.52  ? 224 LYS A CA  1 
ATOM   1902 C  C   . LYS A 1 224 ? -0.207  -10.027 13.764  1.00 11.99  ? 224 LYS A C   1 
ATOM   1903 O  O   . LYS A 1 224 ? -1.079  -9.452  14.427  1.00 13.26  ? 224 LYS A O   1 
ATOM   1904 C  CB  . LYS A 1 224 ? 2.060   -10.572 15.011  1.00 20.79  ? 224 LYS A CB  1 
ATOM   1905 C  CG  . LYS A 1 224 ? 2.672   -11.585 15.995  1.00 22.73  ? 224 LYS A CG  1 
ATOM   1906 C  CD  . LYS A 1 224 ? 4.090   -11.477 16.511  1.00 33.60  ? 224 LYS A CD  1 
ATOM   1907 C  CE  . LYS A 1 224 ? 4.529   -12.827 17.102  1.00 45.38  ? 224 LYS A CE  1 
ATOM   1908 N  NZ  . LYS A 1 224 ? 4.149   -14.054 16.302  1.00 40.83  ? 224 LYS A NZ  1 
ATOM   1909 N  N   . PHE A 1 225 ? -0.133  -9.871  12.446  1.00 11.60  ? 225 PHE A N   1 
ATOM   1910 C  CA  . PHE A 1 225 ? -1.086  -9.006  11.711  1.00 11.32  ? 225 PHE A CA  1 
ATOM   1911 C  C   . PHE A 1 225 ? -2.505  -9.541  11.934  1.00 11.43  ? 225 PHE A C   1 
ATOM   1912 O  O   . PHE A 1 225 ? -3.402  -8.790  12.215  1.00 12.31  ? 225 PHE A O   1 
ATOM   1913 C  CB  . PHE A 1 225 ? -0.836  -9.124  10.182  1.00 11.01  ? 225 PHE A CB  1 
ATOM   1914 C  CG  . PHE A 1 225 ? 0.344   -8.335  9.607   1.00 10.58  ? 225 PHE A CG  1 
ATOM   1915 C  CD1 . PHE A 1 225 ? 1.293   -7.706  10.366  1.00 13.01  ? 225 PHE A CD1 1 
ATOM   1916 C  CD2 . PHE A 1 225 ? 0.486   -8.294  8.218   1.00 11.94  ? 225 PHE A CD2 1 
ATOM   1917 C  CE1 . PHE A 1 225 ? 2.310   -7.017  9.774   1.00 14.89  ? 225 PHE A CE1 1 
ATOM   1918 C  CE2 . PHE A 1 225 ? 1.494   -7.601  7.619   1.00 13.24  ? 225 PHE A CE2 1 
ATOM   1919 C  CZ  . PHE A 1 225 ? 2.408   -6.967  8.403   1.00 11.78  ? 225 PHE A CZ  1 
ATOM   1920 N  N   . ARG A 1 226 ? -2.675  -10.887 11.900  1.00 10.52  ? 226 ARG A N   1 
ATOM   1921 C  CA  . ARG A 1 226 ? -3.991  -11.506 11.954  1.00 11.08  ? 226 ARG A CA  1 
ATOM   1922 C  C   . ARG A 1 226 ? -4.563  -11.538 13.367  1.00 13.19  ? 226 ARG A C   1 
ATOM   1923 O  O   . ARG A 1 226 ? -5.744  -11.926 13.529  1.00 14.86  ? 226 ARG A O   1 
ATOM   1924 C  CB  . ARG A 1 226 ? -3.847  -12.942 11.438  1.00 10.51  ? 226 ARG A CB  1 
ATOM   1925 C  CG  . ARG A 1 226 ? -3.550  -13.061 9.948   1.00 11.86  ? 226 ARG A CG  1 
ATOM   1926 C  CD  . ARG A 1 226 ? -3.547  -14.509 9.537   1.00 15.03  ? 226 ARG A CD  1 
ATOM   1927 N  NE  . ARG A 1 226 ? -3.002  -14.608 8.192   1.00 10.83  ? 226 ARG A NE  1 
ATOM   1928 C  CZ  . ARG A 1 226 ? -2.181  -15.557 7.729   1.00 10.73  ? 226 ARG A CZ  1 
ATOM   1929 N  NH1 . ARG A 1 226 ? -1.757  -16.549 8.499   1.00 15.46  ? 226 ARG A NH1 1 
ATOM   1930 N  NH2 . ARG A 1 226 ? -1.785  -15.488 6.475   1.00 11.56  ? 226 ARG A NH2 1 
ATOM   1931 N  N   . LYS A 1 227 ? -3.807  -11.063 14.366  1.00 11.56  ? 227 LYS A N   1 
ATOM   1932 C  CA  . LYS A 1 227 ? -4.328  -10.944 15.720  1.00 15.08  ? 227 LYS A CA  1 
ATOM   1933 C  C   . LYS A 1 227 ? -4.955  -9.578  16.002  1.00 16.20  ? 227 LYS A C   1 
ATOM   1934 O  O   . LYS A 1 227 ? -5.603  -9.390  17.044  1.00 17.06  ? 227 LYS A O   1 
ATOM   1935 C  CB  . LYS A 1 227 ? -3.273  -11.234 16.789  1.00 14.83  ? 227 LYS A CB  1 
ATOM   1936 C  CG  . LYS A 1 227 ? -2.710  -12.657 16.797  1.00 19.61  ? 227 LYS A CG  1 
ATOM   1937 C  CD  . LYS A 1 227 ? -1.671  -12.885 17.920  1.00 23.50  ? 227 LYS A CD  1 
ATOM   1938 C  CE  . LYS A 1 227 ? -2.383  -13.199 19.238  1.00 30.60  ? 227 LYS A CE  1 
ATOM   1939 N  NZ  . LYS A 1 227 ? -1.519  -13.371 20.442  1.00 48.87  ? 227 LYS A NZ  1 
ATOM   1940 N  N   . LEU A 1 228 ? -4.760  -8.625  15.098  1.00 13.78  ? 228 LEU A N   1 
ATOM   1941 C  CA  . LEU A 1 228 ? -5.431  -7.364  15.201  1.00 15.76  ? 228 LEU A CA  1 
ATOM   1942 C  C   . LEU A 1 228 ? -6.926  -7.529  15.095  1.00 17.15  ? 228 LEU A C   1 
ATOM   1943 O  O   . LEU A 1 228 ? -7.424  -8.575  14.663  1.00 15.45  ? 228 LEU A O   1 
ATOM   1944 C  CB  . LEU A 1 228 ? -4.928  -6.399  14.119  1.00 16.75  ? 228 LEU A CB  1 
ATOM   1945 C  CG  . LEU A 1 228 ? -3.493  -5.934  14.361  1.00 15.20  ? 228 LEU A CG  1 
ATOM   1946 C  CD1 . LEU A 1 228 ? -2.936  -5.263  13.118  1.00 14.80  ? 228 LEU A CD1 1 
ATOM   1947 C  CD2 . LEU A 1 228 ? -3.428  -4.915  15.538  1.00 16.63  ? 228 LEU A CD2 1 
ATOM   1948 N  N   A ASN A 1 229 ? -7.641  -6.488  15.534  0.50 21.24  ? 229 ASN A N   1 
ATOM   1949 N  N   B ASN A 1 229 ? -7.640  -6.482  15.521  0.50 21.25  ? 229 ASN A N   1 
ATOM   1950 C  CA  A ASN A 1 229 ? -9.084  -6.535  15.470  0.50 21.25  ? 229 ASN A CA  1 
ATOM   1951 C  CA  B ASN A 1 229 ? -9.086  -6.519  15.504  0.50 21.34  ? 229 ASN A CA  1 
ATOM   1952 C  C   A ASN A 1 229 ? -9.612  -5.343  14.675  0.50 21.63  ? 229 ASN A C   1 
ATOM   1953 C  C   B ASN A 1 229 ? -9.623  -5.339  14.693  0.50 21.43  ? 229 ASN A C   1 
ATOM   1954 O  O   A ASN A 1 229 ? -9.067  -4.229  14.737  0.50 20.25  ? 229 ASN A O   1 
ATOM   1955 O  O   B ASN A 1 229 ? -9.074  -4.226  14.741  0.50 20.30  ? 229 ASN A O   1 
ATOM   1956 C  CB  A ASN A 1 229 ? -9.747  -6.359  16.845  0.50 24.78  ? 229 ASN A CB  1 
ATOM   1957 C  CB  B ASN A 1 229 ? -9.680  -6.323  16.911  0.50 24.80  ? 229 ASN A CB  1 
ATOM   1958 C  CG  A ASN A 1 229 ? -9.432  -7.428  17.873  0.50 24.10  ? 229 ASN A CG  1 
ATOM   1959 C  CG  B ASN A 1 229 ? -9.747  -7.565  17.784  0.50 23.49  ? 229 ASN A CG  1 
ATOM   1960 O  OD1 A ASN A 1 229 ? -9.652  -7.221  19.065  0.50 29.66  ? 229 ASN A OD1 1 
ATOM   1961 O  OD1 B ASN A 1 229 ? -10.521 -7.615  18.750  0.50 26.37  ? 229 ASN A OD1 1 
ATOM   1962 N  ND2 A ASN A 1 229 ? -8.967  -8.583  17.446  0.50 22.26  ? 229 ASN A ND2 1 
ATOM   1963 N  ND2 B ASN A 1 229 ? -8.912  -8.548  17.515  0.50 21.90  ? 229 ASN A ND2 1 
ATOM   1964 N  N   . PHE A 1 230 ? -10.656 -5.623  13.893  1.00 18.09  ? 230 PHE A N   1 
ATOM   1965 C  CA  . PHE A 1 230 ? -11.445 -4.596  13.195  1.00 20.33  ? 230 PHE A CA  1 
ATOM   1966 C  C   . PHE A 1 230 ? -12.335 -3.795  14.156  1.00 19.86  ? 230 PHE A C   1 
ATOM   1967 O  O   . PHE A 1 230 ? -12.616 -2.639  13.900  1.00 20.00  ? 230 PHE A O   1 
ATOM   1968 C  CB  . PHE A 1 230 ? -12.420 -5.223  12.195  1.00 21.19  ? 230 PHE A CB  1 
ATOM   1969 C  CG  . PHE A 1 230 ? -11.853 -5.773  10.901  1.00 19.87  ? 230 PHE A CG  1 
ATOM   1970 C  CD1 . PHE A 1 230 ? -11.093 -4.989  10.032  1.00 17.42  ? 230 PHE A CD1 1 
ATOM   1971 C  CD2 . PHE A 1 230 ? -12.197 -7.049  10.505  1.00 18.85  ? 230 PHE A CD2 1 
ATOM   1972 C  CE1 . PHE A 1 230 ? -10.668 -5.492  8.804   1.00 17.79  ? 230 PHE A CE1 1 
ATOM   1973 C  CE2 . PHE A 1 230 ? -11.726 -7.581  9.308   1.00 18.61  ? 230 PHE A CE2 1 
ATOM   1974 C  CZ  . PHE A 1 230 ? -10.994 -6.795  8.450   1.00 15.28  ? 230 PHE A CZ  1 
ATOM   1975 N  N   A ASN A 1 231 ? -12.719 -4.412  15.250  0.50 24.59  ? 231 ASN A N   1 
ATOM   1976 N  N   B ASN A 1 231 ? -12.878 -4.476  15.177  0.50 20.61  ? 231 ASN A N   1 
ATOM   1977 C  CA  A ASN A 1 231 ? -13.570 -3.709  16.194  0.50 26.20  ? 231 ASN A CA  1 
ATOM   1978 C  CA  B ASN A 1 231 ? -13.757 -3.875  16.218  0.50 20.68  ? 231 ASN A CA  1 
ATOM   1979 C  C   A ASN A 1 231 ? -12.806 -2.728  17.064  0.50 30.02  ? 231 ASN A C   1 
ATOM   1980 C  C   B ASN A 1 231 ? -12.957 -2.938  17.176  0.50 23.15  ? 231 ASN A C   1 
ATOM   1981 O  O   A ASN A 1 231 ? -11.579 -2.768  17.161  0.50 238.28 ? 231 ASN A O   1 
ATOM   1982 O  O   B ASN A 1 231 ? -11.758 -3.072  17.345  0.50 19.43  ? 231 ASN A O   1 
ATOM   1983 C  CB  A ASN A 1 231 ? -14.073 -4.701  17.212  0.50 20.08  ? 231 ASN A CB  1 
ATOM   1984 C  CB  B ASN A 1 231 ? -14.702 -4.959  16.809  0.50 19.86  ? 231 ASN A CB  1 
ATOM   1985 C  CG  A ASN A 1 231 ? -12.970 -5.570  17.780  0.50 14.38  ? 231 ASN A CG  1 
ATOM   1986 C  CG  B ASN A 1 231 ? -13.996 -6.106  17.492  0.50 10.08  ? 231 ASN A CG  1 
ATOM   1987 O  OD1 A ASN A 1 231 ? -12.422 -6.412  17.048  0.50 13.38  ? 231 ASN A OD1 1 
ATOM   1988 O  OD1 B ASN A 1 231 ? -13.784 -6.052  18.709  0.50 13.97  ? 231 ASN A OD1 1 
ATOM   1989 N  ND2 A ASN A 1 231 ? -12.616 -5.351  19.057  0.50 13.64  ? 231 ASN A ND2 1 
ATOM   1990 N  ND2 B ASN A 1 231 ? -13.443 -6.986  16.696  0.50 8.95   ? 231 ASN A ND2 1 
ATOM   1991 N  N   . GLY A 1 232 ? -13.589 -1.913  17.806  1.00 27.23  ? 232 GLY A N   1 
ATOM   1992 C  CA  . GLY A 1 232 ? -12.958 -1.043  18.834  1.00 29.52  ? 232 GLY A CA  1 
ATOM   1993 C  C   . GLY A 1 232 ? -12.677 -1.764  20.175  1.00 17.30  ? 232 GLY A C   1 
ATOM   1994 O  O   . GLY A 1 232 ? -13.043 -2.884  20.249  1.00 22.95  ? 232 GLY A O   1 
ATOM   1995 N  N   . GLU A 1 233 ? -12.157 -1.122  21.211  1.00 17.96  ? 233 GLU A N   1 
ATOM   1996 C  CA  . GLU A 1 233 ? -12.031 -1.842  22.476  1.00 17.03  ? 233 GLU A CA  1 
ATOM   1997 C  C   . GLU A 1 233 ? -13.479 -1.994  22.968  1.00 23.81  ? 233 GLU A C   1 
ATOM   1998 O  O   . GLU A 1 233 ? -14.063 -1.026  23.456  1.00 20.82  ? 233 GLU A O   1 
ATOM   1999 C  CB  . GLU A 1 233 ? -11.201 -1.046  23.477  1.00 19.07  ? 233 GLU A CB  1 
ATOM   2000 C  CG  . GLU A 1 233 ? -10.652 -1.876  24.627  1.00 18.95  ? 233 GLU A CG  1 
ATOM   2001 C  CD  . GLU A 1 233 ? -9.895  -1.040  25.639  1.00 33.72  ? 233 GLU A CD  1 
ATOM   2002 O  OE1 . GLU A 1 233 ? -9.638  0.150   25.358  1.00 30.18  ? 233 GLU A OE1 1 
ATOM   2003 O  OE2 . GLU A 1 233 ? -9.556  -1.573  26.717  1.00 39.04  ? 233 GLU A OE2 1 
ATOM   2004 N  N   . GLY A 1 234 ? -14.148 -3.116  22.680  1.00 35.04  ? 234 GLY A N   1 
ATOM   2005 C  CA  . GLY A 1 234 ? -15.538 -3.273  23.178  1.00 33.09  ? 234 GLY A CA  1 
ATOM   2006 C  C   . GLY A 1 234 ? -16.713 -3.536  22.214  1.00 50.87  ? 234 GLY A C   1 
ATOM   2007 O  O   . GLY A 1 234 ? -17.706 -2.790  22.321  1.00 57.45  ? 234 GLY A O   1 
ATOM   2008 N  N   . GLU A 1 235 ? -16.635 -4.534  21.317  1.00 48.71  ? 235 GLU A N   1 
ATOM   2009 C  CA  . GLU A 1 235 ? -17.754 -5.061  20.504  1.00 48.31  ? 235 GLU A CA  1 
ATOM   2010 C  C   . GLU A 1 235 ? -17.532 -6.561  20.195  1.00 18.19  ? 235 GLU A C   1 
ATOM   2011 O  O   . GLU A 1 235 ? -16.462 -7.086  20.501  1.00 22.04  ? 235 GLU A O   1 
ATOM   2012 C  CB  . GLU A 1 235 ? -17.903 -4.267  19.207  1.00 57.09  ? 235 GLU A CB  1 
ATOM   2013 C  CG  . GLU A 1 235 ? -17.637 -2.778  19.357  1.00 59.84  ? 235 GLU A CG  1 
ATOM   2014 C  CD  . GLU A 1 235 ? -17.084 -2.155  18.091  1.00 54.69  ? 235 GLU A CD  1 
ATOM   2015 O  OE1 . GLU A 1 235 ? -17.549 -2.524  16.993  1.00 33.43  ? 235 GLU A OE1 1 
ATOM   2016 O  OE2 . GLU A 1 235 ? -16.183 -1.296  18.194  1.00 57.93  ? 235 GLU A OE2 1 
ATOM   2017 N  N   . PRO A 1 236 ? -18.524 -7.266  19.591  1.00 20.68  ? 236 PRO A N   1 
ATOM   2018 C  CA  . PRO A 1 236 ? -18.176 -8.690  19.371  1.00 18.28  ? 236 PRO A CA  1 
ATOM   2019 C  C   . PRO A 1 236 ? -16.831 -8.772  18.576  1.00 15.25  ? 236 PRO A C   1 
ATOM   2020 O  O   . PRO A 1 236 ? -16.617 -8.052  17.560  1.00 21.25  ? 236 PRO A O   1 
ATOM   2021 C  CB  . PRO A 1 236 ? -19.359 -9.337  18.639  1.00 18.44  ? 236 PRO A CB  1 
ATOM   2022 C  CG  . PRO A 1 236 ? -20.504 -8.537  19.174  1.00 21.07  ? 236 PRO A CG  1 
ATOM   2023 C  CD  . PRO A 1 236 ? -19.990 -7.114  19.441  1.00 22.76  ? 236 PRO A CD  1 
ATOM   2024 N  N   . GLU A 1 237 ? -15.736 -9.452  19.052  1.00 26.15  ? 237 GLU A N   1 
ATOM   2025 C  CA  . GLU A 1 237 ? -14.396 -9.507  18.416  1.00 23.29  ? 237 GLU A CA  1 
ATOM   2026 C  C   . GLU A 1 237 ? -14.378 -10.105 17.015  1.00 23.44  ? 237 GLU A C   1 
ATOM   2027 O  O   . GLU A 1 237 ? -14.760 -11.222 16.876  1.00 22.72  ? 237 GLU A O   1 
ATOM   2028 C  CB  . GLU A 1 237 ? -13.477 -10.423 19.250  1.00 26.58  ? 237 GLU A CB  1 
ATOM   2029 C  CG  . GLU A 1 237 ? -12.114 -10.654 18.623  1.00 26.12  ? 237 GLU A CG  1 
ATOM   2030 C  CD  . GLU A 1 237 ? -11.124 -11.390 19.483  1.00 34.36  ? 237 GLU A CD  1 
ATOM   2031 O  OE1 . GLU A 1 237 ? -11.567 -12.046 20.467  1.00 33.29  ? 237 GLU A OE1 1 
ATOM   2032 O  OE2 . GLU A 1 237 ? -9.935  -11.269 19.183  1.00 27.69  ? 237 GLU A OE2 1 
ATOM   2033 N  N   . GLU A 1 238 ? -13.867 -9.370  16.023  1.00 24.46  ? 238 GLU A N   1 
ATOM   2034 C  CA  . GLU A 1 238 ? -13.854 -9.885  14.663  1.00 21.83  ? 238 GLU A CA  1 
ATOM   2035 C  C   . GLU A 1 238 ? -12.364 -9.673  14.223  1.00 20.41  ? 238 GLU A C   1 
ATOM   2036 O  O   . GLU A 1 238 ? -11.871 -8.535  14.196  1.00 18.48  ? 238 GLU A O   1 
ATOM   2037 C  CB  . GLU A 1 238 ? -14.997 -9.327  13.760  1.00 18.38  ? 238 GLU A CB  1 
ATOM   2038 C  CG  . GLU A 1 238 ? -16.433 -9.819  13.845  1.00 21.73  ? 238 GLU A CG  1 
ATOM   2039 C  CD  . GLU A 1 238 ? -17.324 -8.967  12.947  1.00 20.19  ? 238 GLU A CD  1 
ATOM   2040 O  OE1 . GLU A 1 238 ? -17.264 -9.248  11.719  1.00 29.00  ? 238 GLU A OE1 1 
ATOM   2041 O  OE2 . GLU A 1 238 ? -18.016 -8.000  13.426  1.00 31.49  ? 238 GLU A OE2 1 
ATOM   2042 N  N   . LEU A 1 239 ? -11.592 -10.740 13.964  1.00 16.50  ? 239 LEU A N   1 
ATOM   2043 C  CA  . LEU A 1 239 ? -10.175 -10.598 13.611  1.00 13.78  ? 239 LEU A CA  1 
ATOM   2044 C  C   . LEU A 1 239 ? -9.980  -9.779  12.325  1.00 14.18  ? 239 LEU A C   1 
ATOM   2045 O  O   . LEU A 1 239 ? -10.732 -9.941  11.374  1.00 13.93  ? 239 LEU A O   1 
ATOM   2046 C  CB  . LEU A 1 239 ? -9.549  -11.997 13.443  1.00 13.05  ? 239 LEU A CB  1 
ATOM   2047 C  CG  . LEU A 1 239 ? -9.420  -12.827 14.727  1.00 12.01  ? 239 LEU A CG  1 
ATOM   2048 C  CD1 . LEU A 1 239 ? -8.857  -14.176 14.260  1.00 18.50  ? 239 LEU A CD1 1 
ATOM   2049 C  CD2 . LEU A 1 239 ? -8.555  -12.131 15.769  1.00 14.05  ? 239 LEU A CD2 1 
ATOM   2050 N  N   . MET A 1 240 ? -8.952  -8.918  12.317  1.00 13.57  ? 240 MET A N   1 
ATOM   2051 C  CA  . MET A 1 240 ? -8.586  -8.089  11.168  1.00 14.77  ? 240 MET A CA  1 
ATOM   2052 C  C   . MET A 1 240 ? -7.828  -8.989  10.204  1.00 11.74  ? 240 MET A C   1 
ATOM   2053 O  O   . MET A 1 240 ? -6.626  -9.195  10.300  1.00 11.49  ? 240 MET A O   1 
ATOM   2054 C  CB  . MET A 1 240 ? -7.727  -6.905  11.642  1.00 15.05  ? 240 MET A CB  1 
ATOM   2055 C  CG  . MET A 1 240 ? -7.421  -5.948  10.486  1.00 14.36  ? 240 MET A CG  1 
ATOM   2056 S  SD  . MET A 1 240 ? -6.445  -4.530  11.002  1.00 16.09  ? 240 MET A SD  1 
ATOM   2057 C  CE  . MET A 1 240 ? -7.751  -3.461  11.655  1.00 15.79  ? 240 MET A CE  1 
ATOM   2058 N  N   . VAL A 1 241 ? -8.574  -9.567  9.246   1.00 10.99  ? 241 VAL A N   1 
ATOM   2059 C  CA  . VAL A 1 241 ? -8.047  -10.416 8.191   1.00 9.39   ? 241 VAL A CA  1 
ATOM   2060 C  C   . VAL A 1 241 ? -8.853  -10.132 6.942   1.00 8.20   ? 241 VAL A C   1 
ATOM   2061 O  O   . VAL A 1 241 ? -9.986  -9.744  7.024   1.00 9.21   ? 241 VAL A O   1 
ATOM   2062 C  CB  . VAL A 1 241 ? -8.077  -11.920 8.542   1.00 9.49   ? 241 VAL A CB  1 
ATOM   2063 C  CG1 . VAL A 1 241 ? -7.168  -12.216 9.729   1.00 10.85  ? 241 VAL A CG1 1 
ATOM   2064 C  CG2 . VAL A 1 241 ? -9.510  -12.389 8.754   1.00 11.38  ? 241 VAL A CG2 1 
ATOM   2065 N  N   . ASP A 1 242 ? -8.204  -10.391 5.777   1.00 7.89   ? 242 ASP A N   1 
ATOM   2066 C  CA  . ASP A 1 242 ? -8.925  -10.271 4.500   1.00 8.57   ? 242 ASP A CA  1 
ATOM   2067 C  C   . ASP A 1 242 ? -9.412  -8.855  4.233   1.00 8.28   ? 242 ASP A C   1 
ATOM   2068 O  O   . ASP A 1 242 ? -10.539 -8.596  3.827   1.00 9.86   ? 242 ASP A O   1 
ATOM   2069 C  CB  . ASP A 1 242 ? -10.031 -11.340 4.224   1.00 9.23   ? 242 ASP A CB  1 
ATOM   2070 C  CG  . ASP A 1 242 ? -9.440  -12.741 4.159   1.00 8.05   ? 242 ASP A CG  1 
ATOM   2071 O  OD1 . ASP A 1 242 ? -8.382  -12.895 3.509   1.00 7.92   ? 242 ASP A OD1 1 
ATOM   2072 O  OD2 . ASP A 1 242 ? -10.005 -13.645 4.757   1.00 9.67   ? 242 ASP A OD2 1 
ATOM   2073 N  N   . ASN A 1 243 ? -8.546  -7.885  4.500   1.00 7.42   ? 243 ASN A N   1 
ATOM   2074 C  CA  . ASN A 1 243 ? -8.788  -6.461  4.309   1.00 7.81   ? 243 ASN A CA  1 
ATOM   2075 C  C   . ASN A 1 243 ? -8.167  -6.001  2.999   1.00 7.70   ? 243 ASN A C   1 
ATOM   2076 O  O   . ASN A 1 243 ? -7.515  -4.960  2.892   1.00 8.51   ? 243 ASN A O   1 
ATOM   2077 C  CB  . ASN A 1 243 ? -8.208  -5.619  5.472   1.00 8.55   ? 243 ASN A CB  1 
ATOM   2078 C  CG  . ASN A 1 243 ? -6.729  -5.841  5.747   1.00 8.44   ? 243 ASN A CG  1 
ATOM   2079 O  OD1 . ASN A 1 243 ? -6.071  -6.651  5.079   1.00 8.99   ? 243 ASN A OD1 1 
ATOM   2080 N  ND2 . ASN A 1 243 ? -6.139  -5.122  6.724   1.00 10.87  ? 243 ASN A ND2 1 
ATOM   2081 N  N   . TRP A 1 244 ? -8.534  -6.741  1.935   1.00 6.85   ? 244 TRP A N   1 
ATOM   2082 C  CA  . TRP A 1 244 ? -8.013  -6.462  0.603   1.00 6.10   ? 244 TRP A CA  1 
ATOM   2083 C  C   . TRP A 1 244 ? -9.212  -6.363  -0.339  1.00 6.50   ? 244 TRP A C   1 
ATOM   2084 O  O   . TRP A 1 244 ? -10.227 -7.091  -0.229  1.00 8.51   ? 244 TRP A O   1 
ATOM   2085 C  CB  . TRP A 1 244 ? -7.146  -7.604  0.026   1.00 7.07   ? 244 TRP A CB  1 
ATOM   2086 C  CG  . TRP A 1 244 ? -7.602  -9.012  0.219   1.00 6.01   ? 244 TRP A CG  1 
ATOM   2087 C  CD1 . TRP A 1 244 ? -7.496  -9.759  1.308   1.00 6.35   ? 244 TRP A CD1 1 
ATOM   2088 C  CD2 . TRP A 1 244 ? -8.196  -9.857  -0.777  1.00 5.90   ? 244 TRP A CD2 1 
ATOM   2089 N  NE1 . TRP A 1 244 ? -7.980  -11.025 1.103   1.00 6.68   ? 244 TRP A NE1 1 
ATOM   2090 C  CE2 . TRP A 1 244 ? -8.412  -11.109 -0.176  1.00 6.56   ? 244 TRP A CE2 1 
ATOM   2091 C  CE3 . TRP A 1 244 ? -8.488  -9.678  -2.135  1.00 7.13   ? 244 TRP A CE3 1 
ATOM   2092 C  CZ2 . TRP A 1 244 ? -8.985  -12.188 -0.868  1.00 7.67   ? 244 TRP A CZ2 1 
ATOM   2093 C  CZ3 . TRP A 1 244 ? -9.079  -10.733 -2.836  1.00 7.98   ? 244 TRP A CZ3 1 
ATOM   2094 C  CH2 . TRP A 1 244 ? -9.266  -11.960 -2.187  1.00 8.22   ? 244 TRP A CH2 1 
ATOM   2095 N  N   . ARG A 1 245 ? -9.121  -5.487  -1.323  1.00 6.38   ? 245 ARG A N   1 
ATOM   2096 C  CA  . ARG A 1 245 ? -10.052 -5.346  -2.432  1.00 7.55   ? 245 ARG A CA  1 
ATOM   2097 C  C   . ARG A 1 245 ? -9.600  -6.248  -3.554  1.00 7.78   ? 245 ARG A C   1 
ATOM   2098 O  O   . ARG A 1 245 ? -8.405  -6.254  -3.873  1.00 8.23   ? 245 ARG A O   1 
ATOM   2099 C  CB  . ARG A 1 245 ? -10.172 -3.902  -2.897  1.00 7.63   ? 245 ARG A CB  1 
ATOM   2100 C  CG  . ARG A 1 245 ? -11.229 -3.670  -3.976  1.00 8.65   ? 245 ARG A CG  1 
ATOM   2101 C  CD  . ARG A 1 245 ? -11.125 -2.277  -4.581  1.00 10.16  ? 245 ARG A CD  1 
ATOM   2102 N  NE  . ARG A 1 245 ? -12.441 -1.986  -5.233  1.00 9.73   ? 245 ARG A NE  1 
ATOM   2103 C  CZ  . ARG A 1 245 ? -12.635 -0.983  -6.053  1.00 9.11   ? 245 ARG A CZ  1 
ATOM   2104 N  NH1 . ARG A 1 245 ? -11.634 -0.192  -6.464  1.00 8.38   ? 245 ARG A NH1 1 
ATOM   2105 N  NH2 . ARG A 1 245 ? -13.868 -0.736  -6.542  1.00 9.81   ? 245 ARG A NH2 1 
ATOM   2106 N  N   . PRO A 1 246 ? -10.487 -7.063  -4.192  1.00 8.63   ? 246 PRO A N   1 
ATOM   2107 C  CA  . PRO A 1 246 ? -10.029 -7.854  -5.325  1.00 7.94   ? 246 PRO A CA  1 
ATOM   2108 C  C   . PRO A 1 246 ? -9.717  -7.005  -6.561  1.00 9.67   ? 246 PRO A C   1 
ATOM   2109 O  O   . PRO A 1 246 ? -10.063 -5.842  -6.725  1.00 9.90   ? 246 PRO A O   1 
ATOM   2110 C  CB  . PRO A 1 246 ? -11.256 -8.745  -5.651  1.00 10.18  ? 246 PRO A CB  1 
ATOM   2111 C  CG  . PRO A 1 246 ? -12.194 -8.526  -4.576  1.00 17.35  ? 246 PRO A CG  1 
ATOM   2112 C  CD  . PRO A 1 246 ? -11.926 -7.227  -3.868  1.00 13.96  ? 246 PRO A CD  1 
ATOM   2113 N  N   . ALA A 1 247 ? -9.095  -7.691  -7.517  1.00 9.04   ? 247 ALA A N   1 
ATOM   2114 C  CA  . ALA A 1 247 ? -8.704  -7.025  -8.763  1.00 7.43   ? 247 ALA A CA  1 
ATOM   2115 C  C   . ALA A 1 247 ? -9.936  -6.520  -9.489  1.00 7.49   ? 247 ALA A C   1 
ATOM   2116 O  O   . ALA A 1 247 ? -10.996 -7.219  -9.553  1.00 9.31   ? 247 ALA A O   1 
ATOM   2117 C  CB  . ALA A 1 247 ? -7.980  -8.022  -9.669  1.00 8.99   ? 247 ALA A CB  1 
ATOM   2118 N  N   . GLN A 1 248 ? -9.827  -5.364  -10.133 1.00 7.96   ? 248 GLN A N   1 
ATOM   2119 C  CA  . GLN A 1 248 ? -10.839 -4.640  -10.869 1.00 8.83   ? 248 GLN A CA  1 
ATOM   2120 C  C   . GLN A 1 248 ? -10.554 -4.672  -12.330 1.00 9.66   ? 248 GLN A C   1 
ATOM   2121 O  O   . GLN A 1 248 ? -9.389  -4.851  -12.747 1.00 8.92   ? 248 GLN A O   1 
ATOM   2122 C  CB  . GLN A 1 248 ? -10.888 -3.215  -10.276 1.00 9.57   ? 248 GLN A CB  1 
ATOM   2123 C  CG  . GLN A 1 248 ? -11.176 -3.136  -8.784  1.00 9.04   ? 248 GLN A CG  1 
ATOM   2124 C  CD  . GLN A 1 248 ? -12.532 -3.782  -8.475  1.00 10.45  ? 248 GLN A CD  1 
ATOM   2125 O  OE1 . GLN A 1 248 ? -13.572 -3.462  -9.037  1.00 11.23  ? 248 GLN A OE1 1 
ATOM   2126 N  NE2 . GLN A 1 248 ? -12.570 -4.719  -7.534  1.00 9.83   ? 248 GLN A NE2 1 
ATOM   2127 N  N   . PRO A 1 249 ? -11.538 -4.353  -13.193 1.00 10.83  ? 249 PRO A N   1 
ATOM   2128 C  CA  . PRO A 1 249 ? -11.318 -4.356  -14.619 1.00 11.64  ? 249 PRO A CA  1 
ATOM   2129 C  C   . PRO A 1 249 ? -10.216 -3.391  -15.066 1.00 9.06   ? 249 PRO A C   1 
ATOM   2130 O  O   . PRO A 1 249 ? -10.230 -2.196  -14.703 1.00 9.48   ? 249 PRO A O   1 
ATOM   2131 C  CB  . PRO A 1 249 ? -12.693 -4.022  -15.239 1.00 16.83  ? 249 PRO A CB  1 
ATOM   2132 C  CG  . PRO A 1 249 ? -13.644 -4.427  -14.178 1.00 15.81  ? 249 PRO A CG  1 
ATOM   2133 C  CD  . PRO A 1 249 ? -12.970 -4.088  -12.845 1.00 15.86  ? 249 PRO A CD  1 
ATOM   2134 N  N   . LEU A 1 250 ? -9.336  -3.879  -15.932 1.00 10.08  ? 250 LEU A N   1 
ATOM   2135 C  CA  . LEU A 1 250 ? -8.258  -3.028  -16.431 1.00 9.56   ? 250 LEU A CA  1 
ATOM   2136 C  C   . LEU A 1 250 ? -8.816  -1.930  -17.328 1.00 10.69  ? 250 LEU A C   1 
ATOM   2137 O  O   . LEU A 1 250 ? -8.248  -0.832  -17.424 1.00 9.91   ? 250 LEU A O   1 
ATOM   2138 C  CB  . LEU A 1 250 ? -7.273  -3.883  -17.197 1.00 10.72  ? 250 LEU A CB  1 
ATOM   2139 C  CG  . LEU A 1 250 ? -5.993  -3.171  -17.594 1.00 12.03  ? 250 LEU A CG  1 
ATOM   2140 C  CD1 . LEU A 1 250 ? -5.206  -2.624  -16.379 1.00 12.90  ? 250 LEU A CD1 1 
ATOM   2141 C  CD2 . LEU A 1 250 ? -4.996  -4.109  -18.270 1.00 17.92  ? 250 LEU A CD2 1 
ATOM   2142 N  N   . LYS A 1 251 ? -9.866  -2.242  -18.076 1.00 11.56  ? 251 LYS A N   1 
ATOM   2143 C  CA  . LYS A 1 251 ? -10.472 -1.231  -18.948 1.00 14.01  ? 251 LYS A CA  1 
ATOM   2144 C  C   . LYS A 1 251 ? -9.519  -0.709  -20.008 1.00 13.05  ? 251 LYS A C   1 
ATOM   2145 O  O   . LYS A 1 251 ? -8.784  -1.487  -20.620 1.00 16.76  ? 251 LYS A O   1 
ATOM   2146 C  CB  . LYS A 1 251 ? -11.308 -0.203  -18.174 1.00 14.16  ? 251 LYS A CB  1 
ATOM   2147 C  CG  . LYS A 1 251 ? -12.483 -0.841  -17.454 1.00 19.87  ? 251 LYS A CG  1 
ATOM   2148 C  CD  . LYS A 1 251 ? -13.576 0.073   -16.955 1.00 23.45  ? 251 LYS A CD  1 
ATOM   2149 C  CE  . LYS A 1 251 ? -14.622 -0.730  -16.226 1.00 28.94  ? 251 LYS A CE  1 
ATOM   2150 N  NZ  . LYS A 1 251 ? -15.546 0.093   -15.400 1.00 26.30  ? 251 LYS A NZ  1 
ATOM   2151 N  N   . ASN A 1 252 ? -9.392  0.587   -20.168 1.00 12.90  ? 252 ASN A N   1 
ATOM   2152 C  CA  . ASN A 1 252 ? -8.598  1.057   -21.267 1.00 19.03  ? 252 ASN A CA  1 
ATOM   2153 C  C   . ASN A 1 252 ? -7.292  1.543   -20.636 1.00 22.60  ? 252 ASN A C   1 
ATOM   2154 O  O   . ASN A 1 252 ? -7.088  2.804   -20.651 1.00 22.95  ? 252 ASN A O   1 
ATOM   2155 C  CB  . ASN A 1 252 ? -9.364  2.059   -22.167 1.00 23.03  ? 252 ASN A CB  1 
ATOM   2156 C  CG  . ASN A 1 252 ? -8.493  2.631   -23.280 1.00 32.26  ? 252 ASN A CG  1 
ATOM   2157 O  OD1 . ASN A 1 252 ? -7.909  1.866   -24.051 1.00 46.28  ? 252 ASN A OD1 1 
ATOM   2158 N  ND2 . ASN A 1 252 ? -8.321  3.966   -23.357 1.00 30.36  ? 252 ASN A ND2 1 
ATOM   2159 N  N   . ARG A 1 253 ? -6.503  0.564   -20.046 1.00 13.01  ? 253 ARG A N   1 
ATOM   2160 C  CA  . ARG A 1 253 ? -5.223  0.926   -19.458 1.00 10.07  ? 253 ARG A CA  1 
ATOM   2161 C  C   . ARG A 1 253 ? -4.102  0.016   -19.838 1.00 11.01  ? 253 ARG A C   1 
ATOM   2162 O  O   . ARG A 1 253 ? -4.341  -1.126  -20.187 1.00 14.80  ? 253 ARG A O   1 
ATOM   2163 C  CB  . ARG A 1 253 ? -5.289  0.941   -17.949 1.00 9.18   ? 253 ARG A CB  1 
ATOM   2164 C  CG  . ARG A 1 253 ? -6.175  2.076   -17.437 1.00 10.36  ? 253 ARG A CG  1 
ATOM   2165 C  CD  . ARG A 1 253 ? -6.317  2.117   -15.936 1.00 10.24  ? 253 ARG A CD  1 
ATOM   2166 N  NE  . ARG A 1 253 ? -7.137  0.952   -15.473 1.00 9.10   ? 253 ARG A NE  1 
ATOM   2167 C  CZ  . ARG A 1 253 ? -7.410  0.673   -14.213 1.00 8.25   ? 253 ARG A CZ  1 
ATOM   2168 N  NH1 . ARG A 1 253 ? -6.772  1.328   -13.212 1.00 7.99   ? 253 ARG A NH1 1 
ATOM   2169 N  NH2 . ARG A 1 253 ? -8.235  -0.315  -13.881 1.00 8.76   ? 253 ARG A NH2 1 
ATOM   2170 N  N   . GLN A 1 254 ? -2.904  0.546   -19.899 1.00 11.09  ? 254 GLN A N   1 
ATOM   2171 C  CA  . GLN A 1 254 ? -1.713  -0.225  -20.175 1.00 13.38  ? 254 GLN A CA  1 
ATOM   2172 C  C   . GLN A 1 254 ? -0.857  -0.254  -18.897 1.00 10.96  ? 254 GLN A C   1 
ATOM   2173 O  O   . GLN A 1 254 ? -0.633  0.804   -18.237 1.00 15.10  ? 254 GLN A O   1 
ATOM   2174 C  CB  . GLN A 1 254 ? -0.919  0.433   -21.295 1.00 20.98  ? 254 GLN A CB  1 
ATOM   2175 C  CG  . GLN A 1 254 ? -1.664  0.227   -22.616 1.00 31.61  ? 254 GLN A CG  1 
ATOM   2176 C  CD  . GLN A 1 254 ? -0.745  0.356   -23.808 1.00 48.28  ? 254 GLN A CD  1 
ATOM   2177 O  OE1 . GLN A 1 254 ? 0.336   0.905   -23.668 1.00 53.10  ? 254 GLN A OE1 1 
ATOM   2178 N  NE2 . GLN A 1 254 ? -1.200  -0.078  -25.001 1.00 48.56  ? 254 GLN A NE2 1 
ATOM   2179 N  N   . ILE A 1 255 ? -0.401  -1.444  -18.520 1.00 9.45   ? 255 ILE A N   1 
ATOM   2180 C  CA  . ILE A 1 255 ? 0.598   -1.632  -17.490 1.00 8.78   ? 255 ILE A CA  1 
ATOM   2181 C  C   . ILE A 1 255 ? 1.962   -1.662  -18.162 1.00 9.77   ? 255 ILE A C   1 
ATOM   2182 O  O   . ILE A 1 255 ? 2.153   -2.408  -19.149 1.00 11.56  ? 255 ILE A O   1 
ATOM   2183 C  CB  . ILE A 1 255 ? 0.311   -2.867  -16.679 1.00 9.20   ? 255 ILE A CB  1 
ATOM   2184 C  CG1 . ILE A 1 255 ? -1.144  -2.839  -16.130 1.00 10.07  ? 255 ILE A CG1 1 
ATOM   2185 C  CG2 . ILE A 1 255 ? 1.340   -2.974  -15.552 1.00 10.18  ? 255 ILE A CG2 1 
ATOM   2186 C  CD1 . ILE A 1 255 ? -1.433  -4.069  -15.318 1.00 10.58  ? 255 ILE A CD1 1 
ATOM   2187 N  N   . LYS A 1 256 ? 2.852   -0.809  -17.665 1.00 8.62   ? 256 LYS A N   1 
ATOM   2188 C  CA  . LYS A 1 256 ? 4.193   -0.704  -18.209 1.00 8.79   ? 256 LYS A CA  1 
ATOM   2189 C  C   . LYS A 1 256 ? 5.207   -1.291  -17.256 1.00 9.19   ? 256 LYS A C   1 
ATOM   2190 O  O   . LYS A 1 256 ? 5.014   -1.195  -16.051 1.00 11.75  ? 256 LYS A O   1 
ATOM   2191 C  CB  . LYS A 1 256 ? 4.572   0.764   -18.519 1.00 11.65  ? 256 LYS A CB  1 
ATOM   2192 C  CG  . LYS A 1 256 ? 3.587   1.353   -19.523 1.00 17.10  ? 256 LYS A CG  1 
ATOM   2193 C  CD  . LYS A 1 256 ? 3.825   2.763   -19.902 1.00 22.49  ? 256 LYS A CD  1 
ATOM   2194 C  CE  . LYS A 1 256 ? 2.727   3.316   -20.772 1.00 28.91  ? 256 LYS A CE  1 
ATOM   2195 N  NZ  . LYS A 1 256 ? 2.856   4.791   -20.756 1.00 40.67  ? 256 LYS A NZ  1 
ATOM   2196 N  N   . ALA A 1 257 ? 6.227   -1.940  -17.801 1.00 9.97   ? 257 ALA A N   1 
ATOM   2197 C  CA  . ALA A 1 257 ? 7.248   -2.566  -17.002 1.00 11.01  ? 257 ALA A CA  1 
ATOM   2198 C  C   . ALA A 1 257 ? 8.509   -1.718  -17.143 1.00 10.66  ? 257 ALA A C   1 
ATOM   2199 O  O   . ALA A 1 257 ? 8.920   -1.263  -18.248 1.00 12.08  ? 257 ALA A O   1 
ATOM   2200 C  CB  . ALA A 1 257 ? 7.500   -4.006  -17.430 1.00 11.56  ? 257 ALA A CB  1 
ATOM   2201 N  N   . SER A 1 258 ? 9.252   -1.610  -16.045 1.00 9.67   ? 258 SER A N   1 
ATOM   2202 C  CA  . SER A 1 258 ? 10.519  -0.886  -16.046 1.00 11.21  ? 258 SER A CA  1 
ATOM   2203 C  C   . SER A 1 258 ? 11.705  -1.746  -16.441 1.00 12.04  ? 258 SER A C   1 
ATOM   2204 O  O   . SER A 1 258 ? 12.819  -1.217  -16.531 1.00 17.07  ? 258 SER A O   1 
ATOM   2205 C  CB  . SER A 1 258 ? 10.871  -0.329  -14.666 1.00 10.93  ? 258 SER A CB  1 
ATOM   2206 O  OG  . SER A 1 258 ? 11.233  -1.340  -13.777 1.00 11.29  ? 258 SER A OG  1 
ATOM   2207 N  N   . PHE A 1 259 ? 11.394  -2.996  -16.751 1.00 15.19  ? 259 PHE A N   1 
ATOM   2208 C  CA  . PHE A 1 259 ? 12.475  -3.955  -17.011 1.00 16.40  ? 259 PHE A CA  1 
ATOM   2209 C  C   . PHE A 1 259 ? 12.057  -5.033  -17.997 1.00 19.84  ? 259 PHE A C   1 
ATOM   2210 O  O   . PHE A 1 259 ? 10.863  -5.320  -18.217 1.00 19.44  ? 259 PHE A O   1 
ATOM   2211 C  CB  . PHE A 1 259 ? 12.633  -4.793  -15.740 1.00 17.25  ? 259 PHE A CB  1 
ATOM   2212 C  CG  . PHE A 1 259 ? 11.359  -5.505  -15.343 1.00 14.86  ? 259 PHE A CG  1 
ATOM   2213 C  CD1 . PHE A 1 259 ? 10.362  -4.847  -14.638 1.00 13.16  ? 259 PHE A CD1 1 
ATOM   2214 C  CD2 . PHE A 1 259 ? 11.129  -6.823  -15.708 1.00 20.79  ? 259 PHE A CD2 1 
ATOM   2215 C  CE1 . PHE A 1 259 ? 9.185   -5.493  -14.288 1.00 15.16  ? 259 PHE A CE1 1 
ATOM   2216 C  CE2 . PHE A 1 259 ? 9.951   -7.469  -15.357 1.00 19.74  ? 259 PHE A CE2 1 
ATOM   2217 C  CZ  . PHE A 1 259 ? 8.974   -6.805  -14.650 1.00 18.97  ? 259 PHE A CZ  1 
ATOM   2218 N  N   . LYS A 1 260 ? 13.124  -5.600  -18.569 1.00 28.41  ? 260 LYS A N   1 
ATOM   2219 C  CA  . LYS A 1 260 ? 13.427  -6.821  -19.331 1.00 41.51  ? 260 LYS A CA  1 
ATOM   2220 C  C   . LYS A 1 260 ? 13.419  -6.487  -20.828 1.00 44.93  ? 260 LYS A C   1 
ATOM   2221 O  O   . LYS A 1 260 ? 14.476  -6.158  -21.367 1.00 64.70  ? 260 LYS A O   1 
ATOM   2222 C  CB  . LYS A 1 260 ? 12.500  -8.012  -19.051 1.00 44.63  ? 260 LYS A CB  1 
ATOM   2223 C  CG  . LYS A 1 260 ? 13.209  -9.156  -18.323 1.00 66.38  ? 260 LYS A CG  1 
ATOM   2224 C  CD  . LYS A 1 260 ? 12.439  -9.837  -17.176 1.00 71.30  ? 260 LYS A CD  1 
ATOM   2225 C  CE  . LYS A 1 260 ? 10.954  -10.069 -17.444 1.00 68.99  ? 260 LYS A CE  1 
ATOM   2226 N  NZ  . LYS A 1 260 ? 10.457  -11.388 -16.967 1.00 64.83  ? 260 LYS A NZ  1 
ATOM   2227 O  OXT . LYS A 1 260 ? 12.336  -6.567  -21.426 1.00 61.91  ? 260 LYS A OXT 1 
ATOM   2228 C  CA  . HIS B 1 4   ? 0.176   22.240  24.295  1.00 124.04 ? 4   HIS B CA  1 
ATOM   2229 C  C   . HIS B 1 4   ? -0.653  21.310  25.167  1.00 31.01  ? 4   HIS B C   1 
ATOM   2230 O  O   . HIS B 1 4   ? -0.496  20.111  25.022  1.00 34.93  ? 4   HIS B O   1 
ATOM   2231 C  CB  . HIS B 1 4   ? 0.260   23.635  24.897  1.00 83.83  ? 4   HIS B CB  1 
ATOM   2232 C  CG  . HIS B 1 4   ? -0.873  24.497  24.478  1.00 80.95  ? 4   HIS B CG  1 
ATOM   2233 N  ND1 . HIS B 1 4   ? -1.080  25.745  25.046  1.00 96.42  ? 4   HIS B ND1 1 
ATOM   2234 C  CD2 . HIS B 1 4   ? -1.876  24.288  23.582  1.00 109.36 ? 4   HIS B CD2 1 
ATOM   2235 C  CE1 . HIS B 1 4   ? -2.160  26.275  24.502  1.00 108.15 ? 4   HIS B CE1 1 
ATOM   2236 N  NE2 . HIS B 1 4   ? -2.664  25.409  23.610  1.00 108.18 ? 4   HIS B NE2 1 
ATOM   2237 N  N   . TRP B 1 5   ? -1.478  21.881  26.063  1.00 26.63  ? 5   TRP B N   1 
ATOM   2238 C  CA  . TRP B 1 5   ? -2.239  20.992  26.938  1.00 23.84  ? 5   TRP B CA  1 
ATOM   2239 C  C   . TRP B 1 5   ? -3.197  20.158  26.131  1.00 18.13  ? 5   TRP B C   1 
ATOM   2240 O  O   . TRP B 1 5   ? -3.707  20.626  25.091  1.00 24.59  ? 5   TRP B O   1 
ATOM   2241 C  CB  . TRP B 1 5   ? -2.881  21.737  28.113  1.00 18.85  ? 5   TRP B CB  1 
ATOM   2242 C  CG  . TRP B 1 5   ? -4.091  22.551  27.799  1.00 15.24  ? 5   TRP B CG  1 
ATOM   2243 C  CD1 . TRP B 1 5   ? -4.152  23.869  27.451  1.00 18.99  ? 5   TRP B CD1 1 
ATOM   2244 C  CD2 . TRP B 1 5   ? -5.430  22.074  27.764  1.00 14.38  ? 5   TRP B CD2 1 
ATOM   2245 N  NE1 . TRP B 1 5   ? -5.433  24.257  27.213  1.00 19.68  ? 5   TRP B NE1 1 
ATOM   2246 C  CE2 . TRP B 1 5   ? -6.253  23.185  27.451  1.00 16.23  ? 5   TRP B CE2 1 
ATOM   2247 C  CE3 . TRP B 1 5   ? -6.045  20.860  28.084  1.00 13.42  ? 5   TRP B CE3 1 
ATOM   2248 C  CZ2 . TRP B 1 5   ? -7.630  23.109  27.366  1.00 17.64  ? 5   TRP B CZ2 1 
ATOM   2249 C  CZ3 . TRP B 1 5   ? -7.420  20.781  27.957  1.00 13.45  ? 5   TRP B CZ3 1 
ATOM   2250 C  CH2 . TRP B 1 5   ? -8.198  21.889  27.616  1.00 17.01  ? 5   TRP B CH2 1 
ATOM   2251 N  N   . GLY B 1 6   ? -3.491  18.960  26.701  1.00 17.58  ? 6   GLY B N   1 
ATOM   2252 C  CA  . GLY B 1 6   ? -4.554  18.114  26.153  1.00 17.34  ? 6   GLY B CA  1 
ATOM   2253 C  C   . GLY B 1 6   ? -4.863  17.003  27.144  1.00 16.44  ? 6   GLY B C   1 
ATOM   2254 O  O   . GLY B 1 6   ? -4.798  17.181  28.365  1.00 15.87  ? 6   GLY B O   1 
ATOM   2255 N  N   . TYR B 1 7   ? -5.105  15.833  26.555  1.00 17.60  ? 7   TYR B N   1 
ATOM   2256 C  CA  . TYR B 1 7   ? -5.560  14.702  27.363  1.00 18.34  ? 7   TYR B CA  1 
ATOM   2257 C  C   . TYR B 1 7   ? -4.678  13.467  27.209  1.00 26.56  ? 7   TYR B C   1 
ATOM   2258 O  O   . TYR B 1 7   ? -5.093  12.373  27.604  1.00 37.07  ? 7   TYR B O   1 
ATOM   2259 C  CB  . TYR B 1 7   ? -7.045  14.384  27.140  1.00 15.98  ? 7   TYR B CB  1 
ATOM   2260 C  CG  . TYR B 1 7   ? -7.973  15.454  27.665  1.00 11.08  ? 7   TYR B CG  1 
ATOM   2261 C  CD1 . TYR B 1 7   ? -8.339  15.461  29.035  1.00 13.24  ? 7   TYR B CD1 1 
ATOM   2262 C  CD2 . TYR B 1 7   ? -8.436  16.474  26.816  1.00 11.91  ? 7   TYR B CD2 1 
ATOM   2263 C  CE1 . TYR B 1 7   ? -9.142  16.506  29.507  1.00 9.33   ? 7   TYR B CE1 1 
ATOM   2264 C  CE2 . TYR B 1 7   ? -9.261  17.509  27.275  1.00 10.36  ? 7   TYR B CE2 1 
ATOM   2265 C  CZ  . TYR B 1 7   ? -9.605  17.480  28.634  1.00 9.38   ? 7   TYR B CZ  1 
ATOM   2266 O  OH  . TYR B 1 7   ? -10.441 18.463  29.078  1.00 9.41   ? 7   TYR B OH  1 
ATOM   2267 N  N   . GLY B 1 8   ? -3.461  13.667  26.688  1.00 29.36  ? 8   GLY B N   1 
ATOM   2268 C  CA  . GLY B 1 8   ? -2.571  12.523  26.344  1.00 35.75  ? 8   GLY B CA  1 
ATOM   2269 C  C   . GLY B 1 8   ? -1.575  12.202  27.476  1.00 37.46  ? 8   GLY B C   1 
ATOM   2270 O  O   . GLY B 1 8   ? -1.337  13.007  28.422  1.00 32.52  ? 8   GLY B O   1 
ATOM   2271 N  N   . LYS B 1 9   ? -0.789  11.133  27.319  1.00 36.85  ? 9   LYS B N   1 
ATOM   2272 C  CA  . LYS B 1 9   ? 0.275   10.716  28.249  1.00 46.02  ? 9   LYS B CA  1 
ATOM   2273 C  C   . LYS B 1 9   ? 1.291   11.870  28.479  1.00 30.57  ? 9   LYS B C   1 
ATOM   2274 O  O   . LYS B 1 9   ? 1.997   12.035  29.546  1.00 32.47  ? 9   LYS B O   1 
ATOM   2275 C  CB  . LYS B 1 9   ? 0.966   9.494   27.603  1.00 57.95  ? 9   LYS B CB  1 
ATOM   2276 C  CG  . LYS B 1 9   ? 2.175   8.902   28.336  1.00 40.92  ? 9   LYS B CG  1 
ATOM   2277 N  N   . HIS B 1 10  ? 1.381   12.694  27.444  1.00 36.15  ? 10  HIS B N   1 
ATOM   2278 C  CA  . HIS B 1 10  ? 2.501   13.598  27.506  1.00 42.12  ? 10  HIS B CA  1 
ATOM   2279 C  C   . HIS B 1 10  ? 2.041   15.007  27.817  1.00 59.25  ? 10  HIS B C   1 
ATOM   2280 O  O   . HIS B 1 10  ? 2.883   15.821  28.212  1.00 52.27  ? 10  HIS B O   1 
ATOM   2281 C  CB  . HIS B 1 10  ? 3.405   13.467  26.256  1.00 28.10  ? 10  HIS B CB  1 
ATOM   2282 C  CG  . HIS B 1 10  ? 4.193   12.200  26.251  1.00 31.48  ? 10  HIS B CG  1 
ATOM   2283 N  ND1 . HIS B 1 10  ? 5.234   11.956  27.150  1.00 28.43  ? 10  HIS B ND1 1 
ATOM   2284 C  CD2 . HIS B 1 10  ? 3.999   11.067  25.557  1.00 29.64  ? 10  HIS B CD2 1 
ATOM   2285 C  CE1 . HIS B 1 10  ? 5.753   10.773  26.923  1.00 24.35  ? 10  HIS B CE1 1 
ATOM   2286 N  NE2 . HIS B 1 10  ? 4.931   10.165  26.006  1.00 19.72  ? 10  HIS B NE2 1 
ATOM   2287 N  N   . ASN B 1 11  ? 0.704   15.255  27.785  1.00 91.89  ? 11  ASN B N   1 
ATOM   2288 C  CA  . ASN B 1 11  ? 0.256   16.646  27.914  1.00 37.49  ? 11  ASN B CA  1 
ATOM   2289 C  C   . ASN B 1 11  ? -1.102  16.702  28.701  1.00 18.82  ? 11  ASN B C   1 
ATOM   2290 O  O   . ASN B 1 11  ? -1.755  17.747  28.711  1.00 16.51  ? 11  ASN B O   1 
ATOM   2291 C  CB  . ASN B 1 11  ? -0.021  17.351  26.584  1.00 41.09  ? 11  ASN B CB  1 
ATOM   2292 C  CG  . ASN B 1 11  ? -1.054  16.653  25.705  1.00 28.59  ? 11  ASN B CG  1 
ATOM   2293 O  OD1 . ASN B 1 11  ? -1.632  15.617  26.085  1.00 25.61  ? 11  ASN B OD1 1 
ATOM   2294 N  ND2 . ASN B 1 11  ? -1.432  17.270  24.584  1.00 21.95  ? 11  ASN B ND2 1 
ATOM   2295 N  N   . GLY B 1 12  ? -1.459  15.543  29.318  1.00 18.34  ? 12  GLY B N   1 
ATOM   2296 C  CA  . GLY B 1 12  ? -2.747  15.399  29.988  1.00 15.46  ? 12  GLY B CA  1 
ATOM   2297 C  C   . GLY B 1 12  ? -2.721  15.992  31.391  1.00 14.83  ? 12  GLY B C   1 
ATOM   2298 O  O   . GLY B 1 12  ? -1.858  16.706  31.838  1.00 19.44  ? 12  GLY B O   1 
ATOM   2299 N  N   . PRO B 1 13  ? -3.799  15.695  32.153  1.00 12.85  ? 13  PRO B N   1 
ATOM   2300 C  CA  . PRO B 1 13  ? -4.013  16.262  33.474  1.00 14.25  ? 13  PRO B CA  1 
ATOM   2301 C  C   . PRO B 1 13  ? -2.831  16.209  34.438  1.00 13.57  ? 13  PRO B C   1 
ATOM   2302 O  O   . PRO B 1 13  ? -2.764  17.140  35.204  1.00 13.34  ? 13  PRO B O   1 
ATOM   2303 C  CB  . PRO B 1 13  ? -5.250  15.485  33.996  1.00 13.17  ? 13  PRO B CB  1 
ATOM   2304 C  CG  . PRO B 1 13  ? -6.019  15.204  32.760  1.00 13.16  ? 13  PRO B CG  1 
ATOM   2305 C  CD  . PRO B 1 13  ? -4.972  14.954  31.666  1.00 12.74  ? 13  PRO B CD  1 
ATOM   2306 N  N   . GLU B 1 14  ? -2.033  15.140  34.499  1.00 13.96  ? 14  GLU B N   1 
ATOM   2307 C  CA  . GLU B 1 14  ? -0.949  15.114  35.460  1.00 17.70  ? 14  GLU B CA  1 
ATOM   2308 C  C   . GLU B 1 14  ? 0.161   16.089  35.079  1.00 16.19  ? 14  GLU B C   1 
ATOM   2309 O  O   . GLU B 1 14  ? 1.079   16.275  35.886  1.00 18.38  ? 14  GLU B O   1 
ATOM   2310 C  CB  . GLU B 1 14  ? -0.368  13.691  35.528  1.00 24.44  ? 14  GLU B CB  1 
ATOM   2311 C  CG  . GLU B 1 14  ? -1.396  12.623  35.984  1.00 24.04  ? 14  GLU B CG  1 
ATOM   2312 C  CD  . GLU B 1 14  ? -2.327  12.963  37.167  1.00 29.63  ? 14  GLU B CD  1 
ATOM   2313 O  OE1 . GLU B 1 14  ? -3.589  12.891  37.029  1.00 39.65  ? 14  GLU B OE1 1 
ATOM   2314 O  OE2 . GLU B 1 14  ? -1.762  13.344  38.229  1.00 46.06  ? 14  GLU B OE2 1 
ATOM   2315 N  N   . HIS B 1 15  ? 0.069   16.704  33.885  1.00 15.84  ? 15  HIS B N   1 
ATOM   2316 C  CA  . HIS B 1 15  ? 1.083   17.696  33.505  1.00 19.85  ? 15  HIS B CA  1 
ATOM   2317 C  C   . HIS B 1 15  ? 0.666   19.166  33.683  1.00 23.38  ? 15  HIS B C   1 
ATOM   2318 O  O   . HIS B 1 15  ? 1.468   20.135  33.616  1.00 24.40  ? 15  HIS B O   1 
ATOM   2319 C  CB  . HIS B 1 15  ? 1.392   17.501  31.999  1.00 17.06  ? 15  HIS B CB  1 
ATOM   2320 C  CG  . HIS B 1 15  ? 2.241   16.292  31.762  1.00 18.77  ? 15  HIS B CG  1 
ATOM   2321 N  ND1 . HIS B 1 15  ? 3.621   16.299  31.750  1.00 20.63  ? 15  HIS B ND1 1 
ATOM   2322 C  CD2 . HIS B 1 15  ? 1.814   15.004  31.575  1.00 19.81  ? 15  HIS B CD2 1 
ATOM   2323 C  CE1 . HIS B 1 15  ? 4.084   15.095  31.475  1.00 22.58  ? 15  HIS B CE1 1 
ATOM   2324 N  NE2 . HIS B 1 15  ? 3.014   14.265  31.395  1.00 19.63  ? 15  HIS B NE2 1 
ATOM   2325 N  N   . TRP B 1 16  ? -0.632  19.370  33.903  1.00 49.59  ? 16  TRP B N   1 
ATOM   2326 C  CA  . TRP B 1 16  ? -1.195  20.721  33.755  1.00 63.50  ? 16  TRP B CA  1 
ATOM   2327 C  C   . TRP B 1 16  ? -0.517  21.737  34.765  1.00 16.42  ? 16  TRP B C   1 
ATOM   2328 O  O   . TRP B 1 16  ? -0.537  22.933  34.502  1.00 16.22  ? 16  TRP B O   1 
ATOM   2329 C  CB  . TRP B 1 16  ? -2.703  20.706  33.825  1.00 35.97  ? 16  TRP B CB  1 
ATOM   2330 C  CG  . TRP B 1 16  ? -3.393  20.007  32.623  1.00 11.66  ? 16  TRP B CG  1 
ATOM   2331 C  CD1 . TRP B 1 16  ? -2.869  19.553  31.459  1.00 11.09  ? 16  TRP B CD1 1 
ATOM   2332 C  CD2 . TRP B 1 16  ? -4.768  19.670  32.562  1.00 12.48  ? 16  TRP B CD2 1 
ATOM   2333 N  NE1 . TRP B 1 16  ? -3.794  18.968  30.672  1.00 12.25  ? 16  TRP B NE1 1 
ATOM   2334 C  CE2 . TRP B 1 16  ? -5.006  19.023  31.321  1.00 11.97  ? 16  TRP B CE2 1 
ATOM   2335 C  CE3 . TRP B 1 16  ? -5.858  19.833  33.456  1.00 10.79  ? 16  TRP B CE3 1 
ATOM   2336 C  CZ2 . TRP B 1 16  ? -6.292  18.551  30.974  1.00 11.24  ? 16  TRP B CZ2 1 
ATOM   2337 C  CZ3 . TRP B 1 16  ? -7.105  19.370  33.105  1.00 12.85  ? 16  TRP B CZ3 1 
ATOM   2338 C  CH2 . TRP B 1 16  ? -7.317  18.799  31.856  1.00 11.92  ? 16  TRP B CH2 1 
ATOM   2339 N  N   . HIS B 1 17  ? -0.278  21.207  35.969  1.00 18.52  ? 17  HIS B N   1 
ATOM   2340 C  CA  . HIS B 1 17  ? 0.258   22.031  37.072  1.00 15.76  ? 17  HIS B CA  1 
ATOM   2341 C  C   . HIS B 1 17  ? 1.544   22.762  36.632  1.00 16.71  ? 17  HIS B C   1 
ATOM   2342 O  O   . HIS B 1 17  ? 1.699   23.855  37.175  1.00 20.78  ? 17  HIS B O   1 
ATOM   2343 C  CB  . HIS B 1 17  ? 0.512   21.153  38.297  1.00 17.52  ? 17  HIS B CB  1 
ATOM   2344 C  CG  . HIS B 1 17  ? 1.763   20.366  38.145  1.00 16.33  ? 17  HIS B CG  1 
ATOM   2345 N  ND1 . HIS B 1 17  ? 2.968   20.757  38.716  1.00 19.08  ? 17  HIS B ND1 1 
ATOM   2346 C  CD2 . HIS B 1 17  ? 1.980   19.177  37.580  1.00 15.38  ? 17  HIS B CD2 1 
ATOM   2347 C  CE1 . HIS B 1 17  ? 3.888   19.874  38.428  1.00 20.09  ? 17  HIS B CE1 1 
ATOM   2348 N  NE2 . HIS B 1 17  ? 3.326   18.908  37.739  1.00 18.34  ? 17  HIS B NE2 1 
ATOM   2349 N  N   . LYS B 1 18  ? 2.243   22.272  35.550  1.00 18.66  ? 18  LYS B N   1 
ATOM   2350 C  CA  . LYS B 1 18  ? 3.499   23.011  35.211  1.00 17.71  ? 18  LYS B CA  1 
ATOM   2351 C  C   . LYS B 1 18  ? 3.121   24.340  34.566  1.00 23.11  ? 18  LYS B C   1 
ATOM   2352 O  O   . LYS B 1 18  ? 3.817   25.352  34.828  1.00 30.60  ? 18  LYS B O   1 
ATOM   2353 C  CB  . LYS B 1 18  ? 4.357   22.176  34.223  1.00 24.54  ? 18  LYS B CB  1 
ATOM   2354 C  CG  . LYS B 1 18  ? 4.896   20.941  34.889  1.00 21.15  ? 18  LYS B CG  1 
ATOM   2355 C  CD  . LYS B 1 18  ? 5.614   20.019  33.900  1.00 27.69  ? 18  LYS B CD  1 
ATOM   2356 C  CE  . LYS B 1 18  ? 4.574   19.120  33.246  1.00 28.52  ? 18  LYS B CE  1 
ATOM   2357 N  NZ  . LYS B 1 18  ? 5.410   18.243  32.342  1.00 17.99  ? 18  LYS B NZ  1 
ATOM   2358 N  N   . ASP B 1 19  ? 2.087   24.362  33.696  1.00 20.14  ? 19  ASP B N   1 
ATOM   2359 C  CA  . ASP B 1 19  ? 1.634   25.615  33.090  1.00 21.49  ? 19  ASP B CA  1 
ATOM   2360 C  C   . ASP B 1 19  ? 0.671   26.418  33.946  1.00 22.36  ? 19  ASP B C   1 
ATOM   2361 O  O   . ASP B 1 19  ? 0.697   27.717  33.864  1.00 24.63  ? 19  ASP B O   1 
ATOM   2362 C  CB  . ASP B 1 19  ? 1.258   25.570  31.625  1.00 23.25  ? 19  ASP B CB  1 
ATOM   2363 C  CG  . ASP B 1 19  ? 2.401   25.369  30.668  1.00 27.84  ? 19  ASP B CG  1 
ATOM   2364 O  OD1 . ASP B 1 19  ? 3.393   26.005  30.880  1.00 39.71  ? 19  ASP B OD1 1 
ATOM   2365 O  OD2 . ASP B 1 19  ? 2.278   24.527  29.739  1.00 39.41  ? 19  ASP B OD2 1 
ATOM   2366 N  N   . PHE B 1 20  ? -0.052  25.714  34.840  1.00 18.00  ? 20  PHE B N   1 
ATOM   2367 C  CA  . PHE B 1 20  ? -1.180  26.313  35.562  1.00 35.20  ? 20  PHE B CA  1 
ATOM   2368 C  C   . PHE B 1 20  ? -1.034  25.760  37.035  1.00 36.86  ? 20  PHE B C   1 
ATOM   2369 O  O   . PHE B 1 20  ? -1.712  24.779  37.400  1.00 15.65  ? 20  PHE B O   1 
ATOM   2370 C  CB  . PHE B 1 20  ? -2.509  25.897  34.936  1.00 31.52  ? 20  PHE B CB  1 
ATOM   2371 C  CG  . PHE B 1 20  ? -2.604  26.291  33.489  1.00 37.91  ? 20  PHE B CG  1 
ATOM   2372 C  CD1 . PHE B 1 20  ? -2.857  27.606  33.137  1.00 25.47  ? 20  PHE B CD1 1 
ATOM   2373 C  CD2 . PHE B 1 20  ? -2.386  25.360  32.488  1.00 34.44  ? 20  PHE B CD2 1 
ATOM   2374 C  CE1 . PHE B 1 20  ? -2.923  27.977  31.806  1.00 33.14  ? 20  PHE B CE1 1 
ATOM   2375 C  CE2 . PHE B 1 20  ? -2.452  25.732  31.157  1.00 38.34  ? 20  PHE B CE2 1 
ATOM   2376 C  CZ  . PHE B 1 20  ? -2.714  27.039  30.826  1.00 24.76  ? 20  PHE B CZ  1 
ATOM   2377 N  N   . PRO B 1 21  ? -0.178  26.373  37.843  1.00 35.61  ? 21  PRO B N   1 
ATOM   2378 C  CA  . PRO B 1 21  ? 0.041   25.866  39.188  1.00 41.47  ? 21  PRO B CA  1 
ATOM   2379 C  C   . PRO B 1 21  ? -1.197  25.716  40.077  1.00 21.95  ? 21  PRO B C   1 
ATOM   2380 O  O   . PRO B 1 21  ? -1.174  24.959  40.984  1.00 24.23  ? 21  PRO B O   1 
ATOM   2381 C  CB  . PRO B 1 21  ? 1.031   26.870  39.803  1.00 39.24  ? 21  PRO B CB  1 
ATOM   2382 C  CG  . PRO B 1 21  ? 1.147   27.944  38.805  1.00 49.45  ? 21  PRO B CG  1 
ATOM   2383 C  CD  . PRO B 1 21  ? 0.751   27.450  37.483  1.00 36.93  ? 21  PRO B CD  1 
ATOM   2384 N  N   . ILE B 1 22  ? -2.242  26.498  39.799  1.00 13.01  ? 22  ILE B N   1 
ATOM   2385 C  CA  . ILE B 1 22  ? -3.492  26.394  40.553  1.00 12.95  ? 22  ILE B CA  1 
ATOM   2386 C  C   . ILE B 1 22  ? -4.062  24.967  40.427  1.00 12.54  ? 22  ILE B C   1 
ATOM   2387 O  O   . ILE B 1 22  ? -5.043  24.624  41.156  1.00 13.90  ? 22  ILE B O   1 
ATOM   2388 C  CB  . ILE B 1 22  ? -4.441  27.497  40.071  1.00 11.39  ? 22  ILE B CB  1 
ATOM   2389 C  CG1 . ILE B 1 22  ? -5.491  27.795  41.139  1.00 11.92  ? 22  ILE B CG1 1 
ATOM   2390 C  CG2 . ILE B 1 22  ? -5.169  27.162  38.764  1.00 15.30  ? 22  ILE B CG2 1 
ATOM   2391 C  CD1 . ILE B 1 22  ? -6.367  28.935  40.853  1.00 15.30  ? 22  ILE B CD1 1 
ATOM   2392 N  N   . ALA B 1 23  ? -3.557  24.164  39.481  1.00 12.50  ? 23  ALA B N   1 
ATOM   2393 C  CA  . ALA B 1 23  ? -3.987  22.779  39.414  1.00 15.46  ? 23  ALA B CA  1 
ATOM   2394 C  C   . ALA B 1 23  ? -3.937  22.038  40.741  1.00 16.09  ? 23  ALA B C   1 
ATOM   2395 O  O   . ALA B 1 23  ? -4.657  21.027  40.866  1.00 11.39  ? 23  ALA B O   1 
ATOM   2396 C  CB  . ALA B 1 23  ? -3.206  22.014  38.314  1.00 14.73  ? 23  ALA B CB  1 
ATOM   2397 N  N   . LYS B 1 24  ? -2.928  22.420  41.602  1.00 16.36  ? 24  LYS B N   1 
ATOM   2398 C  CA  . LYS B 1 24  ? -2.818  21.822  42.927  1.00 16.09  ? 24  LYS B CA  1 
ATOM   2399 C  C   . LYS B 1 24  ? -3.407  22.763  43.972  1.00 14.64  ? 24  LYS B C   1 
ATOM   2400 O  O   . LYS B 1 24  ? -3.151  22.627  45.149  1.00 18.29  ? 24  LYS B O   1 
ATOM   2401 C  CB  . LYS B 1 24  ? -1.359  21.485  43.229  1.00 16.15  ? 24  LYS B CB  1 
ATOM   2402 C  CG  . LYS B 1 24  ? -0.747  20.567  42.185  1.00 17.27  ? 24  LYS B CG  1 
ATOM   2403 C  CD  . LYS B 1 24  ? 0.688   20.295  42.662  1.00 20.18  ? 24  LYS B CD  1 
ATOM   2404 C  CE  . LYS B 1 24  ? 1.482   19.245  41.899  1.00 25.48  ? 24  LYS B CE  1 
ATOM   2405 N  NZ  . LYS B 1 24  ? 0.758   17.952  41.827  1.00 33.73  ? 24  LYS B NZ  1 
ATOM   2406 N  N   . GLY B 1 25  ? -4.430  23.560  43.592  1.00 15.39  ? 25  GLY B N   1 
ATOM   2407 C  CA  . GLY B 1 25  ? -5.091  24.532  44.475  1.00 14.45  ? 25  GLY B CA  1 
ATOM   2408 C  C   . GLY B 1 25  ? -6.019  23.916  45.533  1.00 12.36  ? 25  GLY B C   1 
ATOM   2409 O  O   . GLY B 1 25  ? -6.237  22.688  45.615  1.00 12.85  ? 25  GLY B O   1 
ATOM   2410 N  N   . GLU B 1 26  ? -6.715  24.823  46.223  1.00 16.47  ? 26  GLU B N   1 
ATOM   2411 C  CA  . GLU B 1 26  ? -7.556  24.420  47.320  1.00 13.32  ? 26  GLU B CA  1 
ATOM   2412 C  C   . GLU B 1 26  ? -9.013  24.200  46.913  1.00 10.26  ? 26  GLU B C   1 
ATOM   2413 O  O   . GLU B 1 26  ? -9.761  23.731  47.745  1.00 12.73  ? 26  GLU B O   1 
ATOM   2414 C  CB  . GLU B 1 26  ? -7.494  25.495  48.407  1.00 17.36  ? 26  GLU B CB  1 
ATOM   2415 C  CG  . GLU B 1 26  ? -6.057  25.746  48.921  1.00 19.96  ? 26  GLU B CG  1 
ATOM   2416 C  CD  . GLU B 1 26  ? -5.486  24.508  49.620  1.00 24.01  ? 26  GLU B CD  1 
ATOM   2417 O  OE1 . GLU B 1 26  ? -6.213  23.836  50.473  1.00 29.50  ? 26  GLU B OE1 1 
ATOM   2418 O  OE2 . GLU B 1 26  ? -4.346  24.177  49.315  1.00 33.79  ? 26  GLU B OE2 1 
ATOM   2419 N  N   . ARG B 1 27  ? -9.414  24.521  45.682  1.00 8.65   ? 27  ARG B N   1 
ATOM   2420 C  CA  . ARG B 1 27  ? -10.796 24.278  45.320  1.00 8.96   ? 27  ARG B CA  1 
ATOM   2421 C  C   . ARG B 1 27  ? -10.879 23.798  43.848  1.00 7.87   ? 27  ARG B C   1 
ATOM   2422 O  O   . ARG B 1 27  ? -11.579 24.409  43.031  1.00 7.81   ? 27  ARG B O   1 
ATOM   2423 C  CB  . ARG B 1 27  ? -11.725 25.455  45.648  1.00 9.59   ? 27  ARG B CB  1 
ATOM   2424 C  CG  . ARG B 1 27  ? -11.290 26.743  44.962  1.00 12.69  ? 27  ARG B CG  1 
ATOM   2425 C  CD  . ARG B 1 27  ? -12.218 27.927  45.236  1.00 10.51  ? 27  ARG B CD  1 
ATOM   2426 N  NE  . ARG B 1 27  ? -13.382 27.857  44.317  1.00 10.06  ? 27  ARG B NE  1 
ATOM   2427 C  CZ  . ARG B 1 27  ? -14.376 28.735  44.296  1.00 9.40   ? 27  ARG B CZ  1 
ATOM   2428 N  NH1 . ARG B 1 27  ? -14.400 29.738  45.165  1.00 10.98  ? 27  ARG B NH1 1 
ATOM   2429 N  NH2 . ARG B 1 27  ? -15.346 28.628  43.433  1.00 10.89  ? 27  ARG B NH2 1 
ATOM   2430 N  N   . GLN B 1 28  ? -10.169 22.730  43.576  1.00 8.38   ? 28  GLN B N   1 
ATOM   2431 C  CA  . GLN B 1 28  ? -10.126 22.211  42.195  1.00 8.03   ? 28  GLN B CA  1 
ATOM   2432 C  C   . GLN B 1 28  ? -11.319 21.265  41.943  1.00 6.99   ? 28  GLN B C   1 
ATOM   2433 O  O   . GLN B 1 28  ? -11.762 20.566  42.828  1.00 7.57   ? 28  GLN B O   1 
ATOM   2434 C  CB  . GLN B 1 28  ? -8.750  21.521  41.961  1.00 10.10  ? 28  GLN B CB  1 
ATOM   2435 C  CG  . GLN B 1 28  ? -7.619  22.565  41.857  1.00 10.59  ? 28  GLN B CG  1 
ATOM   2436 C  CD  . GLN B 1 28  ? -7.748  23.347  40.575  1.00 11.47  ? 28  GLN B CD  1 
ATOM   2437 O  OE1 . GLN B 1 28  ? -7.558  22.799  39.485  1.00 10.20  ? 28  GLN B OE1 1 
ATOM   2438 N  NE2 . GLN B 1 28  ? -8.094  24.624  40.669  1.00 11.07  ? 28  GLN B NE2 1 
ATOM   2439 N  N   . SER B 1 29  ? -11.608 21.138  40.672  1.00 7.80   ? 29  SER B N   1 
ATOM   2440 C  CA  . SER B 1 29  ? -12.693 20.264  40.207  1.00 6.33   ? 29  SER B CA  1 
ATOM   2441 C  C   . SER B 1 29  ? -12.174 19.401  39.109  1.00 6.80   ? 29  SER B C   1 
ATOM   2442 O  O   . SER B 1 29  ? -11.195 19.775  38.382  1.00 7.73   ? 29  SER B O   1 
ATOM   2443 C  CB  . SER B 1 29  ? -13.837 21.107  39.644  1.00 6.04   ? 29  SER B CB  1 
ATOM   2444 O  OG  . SER B 1 29  ? -14.425 21.880  40.680  1.00 6.75   ? 29  SER B OG  1 
ATOM   2445 N  N   . PRO B 1 30  ? -12.799 18.231  38.819  1.00 6.70   ? 30  PRO B N   1 
ATOM   2446 C  CA  . PRO B 1 30  ? -14.006 17.713  39.531  1.00 6.91   ? 30  PRO B CA  1 
ATOM   2447 C  C   . PRO B 1 30  ? -13.595 17.046  40.817  1.00 6.36   ? 30  PRO B C   1 
ATOM   2448 O  O   . PRO B 1 30  ? -12.375 17.007  41.209  1.00 7.52   ? 30  PRO B O   1 
ATOM   2449 C  CB  . PRO B 1 30  ? -14.546 16.688  38.504  1.00 5.95   ? 30  PRO B CB  1 
ATOM   2450 C  CG  . PRO B 1 30  ? -13.188 16.119  37.978  1.00 7.75   ? 30  PRO B CG  1 
ATOM   2451 C  CD  . PRO B 1 30  ? -12.322 17.339  37.774  1.00 8.00   ? 30  PRO B CD  1 
ATOM   2452 N  N   . VAL B 1 31  ? -14.569 16.498  41.542  1.00 6.23   ? 31  VAL B N   1 
ATOM   2453 C  CA  . VAL B 1 31  ? -14.390 15.763  42.768  1.00 7.00   ? 31  VAL B CA  1 
ATOM   2454 C  C   . VAL B 1 31  ? -15.278 14.515  42.723  1.00 6.40   ? 31  VAL B C   1 
ATOM   2455 O  O   . VAL B 1 31  ? -16.217 14.478  41.949  1.00 6.89   ? 31  VAL B O   1 
ATOM   2456 C  CB  . VAL B 1 31  ? -14.708 16.607  44.034  1.00 7.77   ? 31  VAL B CB  1 
ATOM   2457 C  CG1 . VAL B 1 31  ? -13.761 17.795  44.119  1.00 7.82   ? 31  VAL B CG1 1 
ATOM   2458 C  CG2 . VAL B 1 31  ? -16.160 17.087  44.017  1.00 7.85   ? 31  VAL B CG2 1 
ATOM   2459 N  N   . ASP B 1 32  ? -14.951 13.554  43.562  1.00 6.58   ? 32  ASP B N   1 
ATOM   2460 C  CA  . ASP B 1 32  ? -15.914 12.483  43.893  1.00 7.39   ? 32  ASP B CA  1 
ATOM   2461 C  C   . ASP B 1 32  ? -16.927 12.975  44.889  1.00 7.33   ? 32  ASP B C   1 
ATOM   2462 O  O   . ASP B 1 32  ? -16.589 13.667  45.836  1.00 9.11   ? 32  ASP B O   1 
ATOM   2463 C  CB  . ASP B 1 32  ? -15.127 11.322  44.503  1.00 7.72   ? 32  ASP B CB  1 
ATOM   2464 C  CG  . ASP B 1 32  ? -16.061 10.146  44.800  1.00 8.67   ? 32  ASP B CG  1 
ATOM   2465 O  OD1 . ASP B 1 32  ? -16.756 9.683   43.884  1.00 8.56   ? 32  ASP B OD1 1 
ATOM   2466 O  OD2 . ASP B 1 32  ? -16.108 9.733   46.018  1.00 12.01  ? 32  ASP B OD2 1 
ATOM   2467 N  N   . ILE B 1 33  ? -18.155 12.693  44.560  1.00 6.93   ? 33  ILE B N   1 
ATOM   2468 C  CA  . ILE B 1 33  ? -19.277 13.035  45.432  1.00 8.50   ? 33  ILE B CA  1 
ATOM   2469 C  C   . ILE B 1 33  ? -19.595 11.810  46.277  1.00 8.39   ? 33  ILE B C   1 
ATOM   2470 O  O   . ILE B 1 33  ? -20.130 10.814  45.798  1.00 9.16   ? 33  ILE B O   1 
ATOM   2471 C  CB  . ILE B 1 33  ? -20.461 13.475  44.595  1.00 8.22   ? 33  ILE B CB  1 
ATOM   2472 C  CG1 . ILE B 1 33  ? -20.126 14.723  43.775  1.00 8.83   ? 33  ILE B CG1 1 
ATOM   2473 C  CG2 . ILE B 1 33  ? -21.707 13.722  45.533  1.00 9.92   ? 33  ILE B CG2 1 
ATOM   2474 C  CD1 . ILE B 1 33  ? -21.149 15.006  42.605  1.00 9.95   ? 33  ILE B CD1 1 
ATOM   2475 N  N   A ASP B 1 34  ? -19.283 11.917  47.577  0.50 9.10   ? 34  ASP B N   1 
ATOM   2476 N  N   B ASP B 1 34  ? -19.152 11.853  47.546  0.50 10.97  ? 34  ASP B N   1 
ATOM   2477 C  CA  A ASP B 1 34  ? -19.566 10.818  48.481  0.50 10.99  ? 34  ASP B CA  1 
ATOM   2478 C  CA  B ASP B 1 34  ? -19.513 10.796  48.485  0.50 12.19  ? 34  ASP B CA  1 
ATOM   2479 C  C   A ASP B 1 34  ? -20.959 11.076  49.036  0.50 11.23  ? 34  ASP B C   1 
ATOM   2480 C  C   B ASP B 1 34  ? -20.926 11.079  48.996  0.50 12.33  ? 34  ASP B C   1 
ATOM   2481 O  O   A ASP B 1 34  ? -21.178 12.013  49.831  0.50 15.58  ? 34  ASP B O   1 
ATOM   2482 O  O   B ASP B 1 34  ? -21.127 12.037  49.765  0.50 16.04  ? 34  ASP B O   1 
ATOM   2483 C  CB  A ASP B 1 34  ? -18.492 10.724  49.564  0.50 13.70  ? 34  ASP B CB  1 
ATOM   2484 C  CB  B ASP B 1 34  ? -18.489 10.771  49.620  0.50 16.93  ? 34  ASP B CB  1 
ATOM   2485 C  CG  A ASP B 1 34  ? -18.601 9.462   50.404  0.50 12.44  ? 34  ASP B CG  1 
ATOM   2486 C  CG  B ASP B 1 34  ? -18.837 9.824   50.758  0.50 16.71  ? 34  ASP B CG  1 
ATOM   2487 O  OD1 A ASP B 1 34  ? -18.087 8.402   49.967  0.50 16.23  ? 34  ASP B OD1 1 
ATOM   2488 O  OD1 B ASP B 1 34  ? -20.018 9.384   50.856  0.50 17.82  ? 34  ASP B OD1 1 
ATOM   2489 O  OD2 A ASP B 1 34  ? -19.210 9.524   51.492  0.50 12.65  ? 34  ASP B OD2 1 
ATOM   2490 O  OD2 B ASP B 1 34  ? -17.905 9.527   51.551  0.50 19.08  ? 34  ASP B OD2 1 
ATOM   2491 N  N   . THR B 1 35  ? -21.908 10.279  48.560  1.00 11.96  ? 35  THR B N   1 
ATOM   2492 C  CA  . THR B 1 35  ? -23.317 10.579  48.794  1.00 15.69  ? 35  THR B CA  1 
ATOM   2493 C  C   . THR B 1 35  ? -23.651 10.479  50.276  1.00 15.57  ? 35  THR B C   1 
ATOM   2494 O  O   . THR B 1 35  ? -24.549 11.141  50.725  1.00 19.23  ? 35  THR B O   1 
ATOM   2495 C  CB  . THR B 1 35  ? -24.167 9.611   47.981  1.00 16.46  ? 35  THR B CB  1 
ATOM   2496 O  OG1 . THR B 1 35  ? -24.036 8.266   48.452  1.00 17.08  ? 35  THR B OG1 1 
ATOM   2497 C  CG2 . THR B 1 35  ? -23.991 9.746   46.485  1.00 16.12  ? 35  THR B CG2 1 
ATOM   2498 N  N   A HIS B 1 36  ? -22.946 9.615   50.982  0.50 19.42  ? 36  HIS B N   1 
ATOM   2499 N  N   B HIS B 1 36  ? -22.841 9.700   51.028  0.50 19.65  ? 36  HIS B N   1 
ATOM   2500 C  CA  A HIS B 1 36  ? -23.306 9.454   52.360  0.50 19.26  ? 36  HIS B CA  1 
ATOM   2501 C  CA  B HIS B 1 36  ? -22.984 9.335   52.445  0.50 21.15  ? 36  HIS B CA  1 
ATOM   2502 C  C   A HIS B 1 36  ? -22.807 10.659  53.155  0.50 17.59  ? 36  HIS B C   1 
ATOM   2503 C  C   B HIS B 1 36  ? -22.308 10.367  53.346  0.50 21.34  ? 36  HIS B C   1 
ATOM   2504 O  O   A HIS B 1 36  ? -23.433 10.942  54.157  0.50 13.43  ? 36  HIS B O   1 
ATOM   2505 O  O   B HIS B 1 36  ? -22.254 10.292  54.561  0.50 24.90  ? 36  HIS B O   1 
ATOM   2506 C  CB  A HIS B 1 36  ? -22.992 8.041   52.874  0.50 17.78  ? 36  HIS B CB  1 
ATOM   2507 C  CB  B HIS B 1 36  ? -22.329 7.980   52.723  0.50 22.82  ? 36  HIS B CB  1 
ATOM   2508 C  CG  A HIS B 1 36  ? -23.876 6.973   52.292  0.50 16.67  ? 36  HIS B CG  1 
ATOM   2509 C  CG  B HIS B 1 36  ? -22.973 6.837   52.018  0.50 24.66  ? 36  HIS B CG  1 
ATOM   2510 N  ND1 A HIS B 1 36  ? -25.193 6.823   52.694  0.50 16.27  ? 36  HIS B ND1 1 
ATOM   2511 N  ND1 B HIS B 1 36  ? -22.392 6.197   50.941  0.50 21.15  ? 36  HIS B ND1 1 
ATOM   2512 C  CD2 A HIS B 1 36  ? -23.677 6.039   51.320  0.50 17.31  ? 36  HIS B CD2 1 
ATOM   2513 C  CD2 B HIS B 1 36  ? -24.142 6.203   52.241  0.50 30.79  ? 36  HIS B CD2 1 
ATOM   2514 C  CE1 A HIS B 1 36  ? -25.756 5.818   52.048  0.50 21.10  ? 36  HIS B CE1 1 
ATOM   2515 C  CE1 B HIS B 1 36  ? -23.174 5.239   50.533  0.50 23.65  ? 36  HIS B CE1 1 
ATOM   2516 N  NE2 A HIS B 1 36  ? -24.856 5.334   51.186  0.50 21.41  ? 36  HIS B NE2 1 
ATOM   2517 N  NE2 B HIS B 1 36  ? -24.256 5.223   51.295  0.50 26.88  ? 36  HIS B NE2 1 
ATOM   2518 N  N   . THR B 1 37  ? -21.717 11.333  52.704  1.00 18.60  ? 37  THR B N   1 
ATOM   2519 C  CA  . THR B 1 37  ? -21.098 12.460  53.383  1.00 20.04  ? 37  THR B CA  1 
ATOM   2520 C  C   . THR B 1 37  ? -21.728 13.803  53.012  1.00 18.47  ? 37  THR B C   1 
ATOM   2521 O  O   . THR B 1 37  ? -21.675 14.761  53.804  1.00 25.70  ? 37  THR B O   1 
ATOM   2522 C  CB  . THR B 1 37  ? -19.574 12.407  53.258  1.00 22.97  ? 37  THR B CB  1 
ATOM   2523 O  OG1 . THR B 1 37  ? -19.272 11.086  53.726  1.00 26.59  ? 37  THR B OG1 1 
ATOM   2524 C  CG2 . THR B 1 37  ? -18.858 13.476  54.089  1.00 27.18  ? 37  THR B CG2 1 
ATOM   2525 N  N   . ALA B 1 38  ? -22.356 13.882  51.847  1.00 15.44  ? 38  ALA B N   1 
ATOM   2526 C  CA  . ALA B 1 38  ? -22.941 15.156  51.448  1.00 14.53  ? 38  ALA B CA  1 
ATOM   2527 C  C   . ALA B 1 38  ? -24.131 15.411  52.352  1.00 22.52  ? 38  ALA B C   1 
ATOM   2528 O  O   . ALA B 1 38  ? -24.939 14.544  52.661  1.00 27.52  ? 38  ALA B O   1 
ATOM   2529 C  CB  . ALA B 1 38  ? -23.346 15.093  50.023  1.00 15.29  ? 38  ALA B CB  1 
ATOM   2530 N  N   A LYS B 1 39  ? -24.195 16.592  52.950  0.50 21.91  ? 39  LYS B N   1 
ATOM   2531 N  N   B LYS B 1 39  ? -24.254 16.647  52.774  0.50 22.45  ? 39  LYS B N   1 
ATOM   2532 C  CA  A LYS B 1 39  ? -25.357 16.758  53.825  0.50 21.78  ? 39  LYS B CA  1 
ATOM   2533 C  CA  B LYS B 1 39  ? -25.298 16.844  53.756  0.50 21.25  ? 39  LYS B CA  1 
ATOM   2534 C  C   A LYS B 1 39  ? -26.482 17.553  53.176  0.50 15.35  ? 39  LYS B C   1 
ATOM   2535 C  C   B LYS B 1 39  ? -26.493 17.589  53.168  0.50 15.49  ? 39  LYS B C   1 
ATOM   2536 O  O   A LYS B 1 39  ? -26.271 18.521  52.426  0.50 16.23  ? 39  LYS B O   1 
ATOM   2537 O  O   B LYS B 1 39  ? -26.337 18.561  52.415  0.50 16.35  ? 39  LYS B O   1 
ATOM   2538 C  CB  A LYS B 1 39  ? -25.061 17.173  55.268  0.50 19.94  ? 39  LYS B CB  1 
ATOM   2539 C  CB  B LYS B 1 39  ? -24.698 17.417  55.030  0.50 24.44  ? 39  LYS B CB  1 
ATOM   2540 C  CG  A LYS B 1 39  ? -26.265 17.217  56.218  0.50 17.96  ? 39  LYS B CG  1 
ATOM   2541 C  CG  B LYS B 1 39  ? -24.700 18.932  55.159  0.50 21.71  ? 39  LYS B CG  1 
ATOM   2542 C  CD  A LYS B 1 39  ? -26.608 18.626  56.611  0.50 28.85  ? 39  LYS B CD  1 
ATOM   2543 C  CD  B LYS B 1 39  ? -24.891 19.251  56.618  0.50 26.15  ? 39  LYS B CD  1 
ATOM   2544 C  CE  A LYS B 1 39  ? -25.843 19.090  57.836  0.50 25.05  ? 39  LYS B CE  1 
ATOM   2545 C  CE  B LYS B 1 39  ? -25.601 18.122  57.343  0.50 23.73  ? 39  LYS B CE  1 
ATOM   2546 N  NZ  A LYS B 1 39  ? -26.375 18.472  59.103  0.50 28.61  ? 39  LYS B NZ  1 
ATOM   2547 N  NZ  B LYS B 1 39  ? -26.260 18.587  58.591  0.50 34.09  ? 39  LYS B NZ  1 
ATOM   2548 N  N   . TYR B 1 40  ? -27.691 17.086  53.425  1.00 18.20  ? 40  TYR B N   1 
ATOM   2549 C  CA  . TYR B 1 40  ? -28.878 17.786  53.024  1.00 14.84  ? 40  TYR B CA  1 
ATOM   2550 C  C   . TYR B 1 40  ? -28.931 19.162  53.676  1.00 14.46  ? 40  TYR B C   1 
ATOM   2551 O  O   . TYR B 1 40  ? -28.792 19.289  54.892  1.00 15.91  ? 40  TYR B O   1 
ATOM   2552 C  CB  . TYR B 1 40  ? -30.134 16.996  53.414  1.00 21.94  ? 40  TYR B CB  1 
ATOM   2553 C  CG  . TYR B 1 40  ? -31.374 17.797  53.243  1.00 22.43  ? 40  TYR B CG  1 
ATOM   2554 C  CD1 . TYR B 1 40  ? -31.779 18.232  51.995  1.00 20.53  ? 40  TYR B CD1 1 
ATOM   2555 C  CD2 . TYR B 1 40  ? -32.170 18.088  54.349  1.00 28.17  ? 40  TYR B CD2 1 
ATOM   2556 C  CE1 . TYR B 1 40  ? -32.946 18.950  51.820  1.00 23.50  ? 40  TYR B CE1 1 
ATOM   2557 C  CE2 . TYR B 1 40  ? -33.345 18.807  54.182  1.00 28.72  ? 40  TYR B CE2 1 
ATOM   2558 C  CZ  . TYR B 1 40  ? -33.747 19.218  52.921  1.00 26.26  ? 40  TYR B CZ  1 
ATOM   2559 O  OH  . TYR B 1 40  ? -34.922 19.909  52.740  1.00 31.37  ? 40  TYR B OH  1 
ATOM   2560 N  N   . ASP B 1 41  ? -29.079 20.173  52.858  1.00 12.76  ? 41  ASP B N   1 
ATOM   2561 C  CA  . ASP B 1 41  ? -29.096 21.570  53.284  1.00 13.83  ? 41  ASP B CA  1 
ATOM   2562 C  C   . ASP B 1 41  ? -30.500 22.112  53.015  1.00 14.40  ? 41  ASP B C   1 
ATOM   2563 O  O   . ASP B 1 41  ? -30.779 22.519  51.918  1.00 17.63  ? 41  ASP B O   1 
ATOM   2564 C  CB  . ASP B 1 41  ? -27.984 22.369  52.604  1.00 16.23  ? 41  ASP B CB  1 
ATOM   2565 C  CG  . ASP B 1 41  ? -27.942 23.785  53.153  1.00 20.64  ? 41  ASP B CG  1 
ATOM   2566 O  OD1 . ASP B 1 41  ? -28.908 24.194  53.882  1.00 22.93  ? 41  ASP B OD1 1 
ATOM   2567 O  OD2 . ASP B 1 41  ? -27.020 24.482  52.830  1.00 23.88  ? 41  ASP B OD2 1 
ATOM   2568 N  N   . PRO B 1 42  ? -31.377 22.181  54.034  1.00 20.17  ? 42  PRO B N   1 
ATOM   2569 C  CA  . PRO B 1 42  ? -32.800 22.567  53.826  1.00 24.50  ? 42  PRO B CA  1 
ATOM   2570 C  C   . PRO B 1 42  ? -32.884 24.060  53.444  1.00 24.18  ? 42  PRO B C   1 
ATOM   2571 O  O   . PRO B 1 42  ? -33.951 24.530  53.001  1.00 29.11  ? 42  PRO B O   1 
ATOM   2572 C  CB  . PRO B 1 42  ? -33.463 22.210  55.176  1.00 26.14  ? 42  PRO B CB  1 
ATOM   2573 C  CG  . PRO B 1 42  ? -32.330 22.384  56.150  1.00 29.83  ? 42  PRO B CG  1 
ATOM   2574 C  CD  . PRO B 1 42  ? -31.113 21.789  55.447  1.00 23.77  ? 42  PRO B CD  1 
ATOM   2575 N  N   . SER B 1 43  ? -31.773 24.805  53.633  1.00 21.49  ? 43  SER B N   1 
ATOM   2576 C  CA  . SER B 1 43  ? -31.736 26.237  53.258  1.00 26.89  ? 43  SER B CA  1 
ATOM   2577 C  C   . SER B 1 43  ? -31.559 26.443  51.744  1.00 21.94  ? 43  SER B C   1 
ATOM   2578 O  O   . SER B 1 43  ? -31.882 27.525  51.245  1.00 30.68  ? 43  SER B O   1 
ATOM   2579 C  CB  . SER B 1 43  ? -30.678 27.077  53.989  1.00 33.60  ? 43  SER B CB  1 
ATOM   2580 O  OG  . SER B 1 43  ? -29.371 26.688  53.666  1.00 26.57  ? 43  SER B OG  1 
ATOM   2581 N  N   . LEU B 1 44  ? -31.103 25.426  51.006  1.00 25.67  ? 44  LEU B N   1 
ATOM   2582 C  CA  . LEU B 1 44  ? -30.866 25.609  49.574  1.00 23.27  ? 44  LEU B CA  1 
ATOM   2583 C  C   . LEU B 1 44  ? -32.218 25.734  48.896  1.00 27.74  ? 44  LEU B C   1 
ATOM   2584 O  O   . LEU B 1 44  ? -33.163 25.155  49.369  1.00 27.31  ? 44  LEU B O   1 
ATOM   2585 C  CB  . LEU B 1 44  ? -30.201 24.366  49.005  1.00 18.68  ? 44  LEU B CB  1 
ATOM   2586 C  CG  . LEU B 1 44  ? -28.681 24.234  49.211  1.00 20.34  ? 44  LEU B CG  1 
ATOM   2587 C  CD1 . LEU B 1 44  ? -28.279 22.854  48.723  1.00 17.00  ? 44  LEU B CD1 1 
ATOM   2588 C  CD2 . LEU B 1 44  ? -27.921 25.272  48.437  1.00 15.52  ? 44  LEU B CD2 1 
ATOM   2589 N  N   . LYS B 1 45  ? -32.216 26.368  47.718  1.00 21.29  ? 45  LYS B N   1 
ATOM   2590 C  CA  . LYS B 1 45  ? -33.447 26.626  47.003  1.00 23.32  ? 45  LYS B CA  1 
ATOM   2591 C  C   . LYS B 1 45  ? -33.551 25.671  45.813  1.00 23.22  ? 45  LYS B C   1 
ATOM   2592 O  O   . LYS B 1 45  ? -32.509 25.008  45.459  1.00 25.09  ? 45  LYS B O   1 
ATOM   2593 C  CB  . LYS B 1 45  ? -33.468 28.083  46.616  1.00 22.11  ? 45  LYS B CB  1 
ATOM   2594 C  CG  . LYS B 1 45  ? -33.368 29.011  47.818  1.00 25.77  ? 45  LYS B CG  1 
ATOM   2595 C  CD  . LYS B 1 45  ? -33.245 30.507  47.534  1.00 37.78  ? 45  LYS B CD  1 
ATOM   2596 C  CE  . LYS B 1 45  ? -34.499 31.189  48.081  1.00 45.74  ? 45  LYS B CE  1 
ATOM   2597 N  N   . PRO B 1 46  ? -34.805 25.489  45.275  1.00 22.37  ? 46  PRO B N   1 
ATOM   2598 C  CA  . PRO B 1 46  ? -34.815 24.777  43.988  1.00 28.21  ? 46  PRO B CA  1 
ATOM   2599 C  C   . PRO B 1 46  ? -34.011 25.612  43.017  1.00 18.97  ? 46  PRO B C   1 
ATOM   2600 O  O   . PRO B 1 46  ? -34.041 26.839  43.030  1.00 21.97  ? 46  PRO B O   1 
ATOM   2601 C  CB  . PRO B 1 46  ? -36.277 24.892  43.571  1.00 27.34  ? 46  PRO B CB  1 
ATOM   2602 C  CG  . PRO B 1 46  ? -37.007 25.028  44.892  1.00 25.46  ? 46  PRO B CG  1 
ATOM   2603 C  CD  . PRO B 1 46  ? -36.142 25.831  45.819  1.00 21.43  ? 46  PRO B CD  1 
ATOM   2604 N  N   . LEU B 1 47  ? -33.437 24.883  42.079  1.00 20.94  ? 47  LEU B N   1 
ATOM   2605 C  CA  . LEU B 1 47  ? -32.685 25.554  41.072  1.00 16.58  ? 47  LEU B CA  1 
ATOM   2606 C  C   . LEU B 1 47  ? -33.754 26.154  40.130  1.00 18.75  ? 47  LEU B C   1 
ATOM   2607 O  O   . LEU B 1 47  ? -34.847 25.590  39.967  1.00 23.56  ? 47  LEU B O   1 
ATOM   2608 C  CB  . LEU B 1 47  ? -31.887 24.402  40.421  1.00 28.19  ? 47  LEU B CB  1 
ATOM   2609 C  CG  . LEU B 1 47  ? -30.983 24.709  39.132  1.00 31.99  ? 47  LEU B CG  1 
ATOM   2610 C  CD1 . LEU B 1 47  ? -29.742 25.632  39.619  1.00 43.87  ? 47  LEU B CD1 1 
ATOM   2611 C  CD2 . LEU B 1 47  ? -30.459 23.366  38.706  1.00 27.86  ? 47  LEU B CD2 1 
ATOM   2612 N  N   . SER B 1 48  ? -33.541 27.325  39.525  1.00 17.14  ? 48  SER B N   1 
ATOM   2613 C  CA  . SER B 1 48  ? -34.393 27.896  38.466  1.00 13.93  ? 48  SER B CA  1 
ATOM   2614 C  C   . SER B 1 48  ? -33.554 27.886  37.178  1.00 15.50  ? 48  SER B C   1 
ATOM   2615 O  O   . SER B 1 48  ? -32.539 28.635  37.034  1.00 15.83  ? 48  SER B O   1 
ATOM   2616 C  CB  . SER B 1 48  ? -34.683 29.348  38.818  1.00 15.67  ? 48  SER B CB  1 
ATOM   2617 O  OG  . SER B 1 48  ? -35.382 30.007  37.800  1.00 19.86  ? 48  SER B OG  1 
ATOM   2618 N  N   . VAL B 1 49  ? -33.932 27.041  36.240  1.00 15.79  ? 49  VAL B N   1 
ATOM   2619 C  CA  . VAL B 1 49  ? -33.280 26.980  34.905  1.00 19.26  ? 49  VAL B CA  1 
ATOM   2620 C  C   . VAL B 1 49  ? -34.333 27.556  33.941  1.00 18.82  ? 49  VAL B C   1 
ATOM   2621 O  O   . VAL B 1 49  ? -35.406 27.005  33.782  1.00 23.91  ? 49  VAL B O   1 
ATOM   2622 C  CB  . VAL B 1 49  ? -32.734 25.572  34.468  1.00 31.24  ? 49  VAL B CB  1 
ATOM   2623 C  CG1 . VAL B 1 49  ? -31.762 25.717  33.308  1.00 42.62  ? 49  VAL B CG1 1 
ATOM   2624 C  CG2 . VAL B 1 49  ? -32.071 24.872  35.644  1.00 29.47  ? 49  VAL B CG2 1 
ATOM   2625 N  N   . SER B 1 50  ? -34.045 28.752  33.450  1.00 19.27  ? 50  SER B N   1 
ATOM   2626 C  CA  . SER B 1 50  ? -34.924 29.504  32.575  1.00 22.60  ? 50  SER B CA  1 
ATOM   2627 C  C   . SER B 1 50  ? -34.348 29.584  31.184  1.00 21.77  ? 50  SER B C   1 
ATOM   2628 O  O   . SER B 1 50  ? -33.545 30.492  30.905  1.00 22.41  ? 50  SER B O   1 
ATOM   2629 C  CB  . SER B 1 50  ? -35.116 30.881  33.131  1.00 28.75  ? 50  SER B CB  1 
ATOM   2630 O  OG  . SER B 1 50  ? -36.119 30.832  34.118  1.00 41.80  ? 50  SER B OG  1 
ATOM   2631 N  N   . TYR B 1 51  ? -34.625 28.527  30.401  1.00 21.23  ? 51  TYR B N   1 
ATOM   2632 C  CA  . TYR B 1 51  ? -34.032 28.326  29.101  1.00 23.16  ? 51  TYR B CA  1 
ATOM   2633 C  C   . TYR B 1 51  ? -35.008 28.618  27.969  1.00 23.52  ? 51  TYR B C   1 
ATOM   2634 O  O   . TYR B 1 51  ? -34.600 28.499  26.802  1.00 21.86  ? 51  TYR B O   1 
ATOM   2635 C  CB  . TYR B 1 51  ? -33.420 26.922  28.973  1.00 23.12  ? 51  TYR B CB  1 
ATOM   2636 C  CG  . TYR B 1 51  ? -32.168 26.654  29.786  1.00 15.31  ? 51  TYR B CG  1 
ATOM   2637 C  CD1 . TYR B 1 51  ? -31.416 27.662  30.405  1.00 14.26  ? 51  TYR B CD1 1 
ATOM   2638 C  CD2 . TYR B 1 51  ? -31.659 25.387  29.837  1.00 14.27  ? 51  TYR B CD2 1 
ATOM   2639 C  CE1 . TYR B 1 51  ? -30.197 27.379  31.032  1.00 14.78  ? 51  TYR B CE1 1 
ATOM   2640 C  CE2 . TYR B 1 51  ? -30.416 25.110  30.392  1.00 13.54  ? 51  TYR B CE2 1 
ATOM   2641 C  CZ  . TYR B 1 51  ? -29.681 26.094  31.048  1.00 14.17  ? 51  TYR B CZ  1 
ATOM   2642 O  OH  . TYR B 1 51  ? -28.527 25.735  31.669  1.00 13.35  ? 51  TYR B OH  1 
ATOM   2643 N  N   . ASP B 1 52  ? -36.331 28.924  28.276  1.00 37.17  ? 52  ASP B N   1 
ATOM   2644 C  CA  . ASP B 1 52  ? -37.345 29.305  27.257  1.00 35.30  ? 52  ASP B CA  1 
ATOM   2645 C  C   . ASP B 1 52  ? -36.810 30.206  26.130  1.00 34.34  ? 52  ASP B C   1 
ATOM   2646 O  O   . ASP B 1 52  ? -37.122 29.987  24.962  1.00 36.41  ? 52  ASP B O   1 
ATOM   2647 C  CB  . ASP B 1 52  ? -38.595 29.968  27.877  1.00 34.53  ? 52  ASP B CB  1 
ATOM   2648 C  CG  . ASP B 1 52  ? -39.845 29.998  26.990  1.00 56.20  ? 52  ASP B CG  1 
ATOM   2649 O  OD1 . ASP B 1 52  ? -39.856 29.350  25.911  1.00 60.61  ? 52  ASP B OD1 1 
ATOM   2650 O  OD2 . ASP B 1 52  ? -40.828 30.661  27.406  1.00 79.51  ? 52  ASP B OD2 1 
ATOM   2651 N  N   . GLN B 1 53  ? -36.019 31.226  26.480  1.00 29.53  ? 53  GLN B N   1 
ATOM   2652 C  CA  . GLN B 1 53  ? -35.643 32.226  25.465  1.00 31.28  ? 53  GLN B CA  1 
ATOM   2653 C  C   . GLN B 1 53  ? -34.245 31.986  24.880  1.00 20.48  ? 53  GLN B C   1 
ATOM   2654 O  O   . GLN B 1 53  ? -33.630 32.884  24.297  1.00 25.87  ? 53  GLN B O   1 
ATOM   2655 C  CB  . GLN B 1 53  ? -35.759 33.661  26.015  1.00 41.00  ? 53  GLN B CB  1 
ATOM   2656 C  CG  . GLN B 1 53  ? -37.195 34.150  26.151  1.00 45.05  ? 53  GLN B CG  1 
ATOM   2657 C  CD  . GLN B 1 53  ? -38.107 33.930  24.955  1.00 51.26  ? 53  GLN B CD  1 
ATOM   2658 O  OE1 . GLN B 1 53  ? -37.804 34.297  23.816  1.00 64.52  ? 53  GLN B OE1 1 
ATOM   2659 N  NE2 . GLN B 1 53  ? -39.276 33.391  25.215  1.00 47.47  ? 53  GLN B NE2 1 
ATOM   2660 N  N   . ALA B 1 54  ? -33.722 30.783  25.064  1.00 21.95  ? 54  ALA B N   1 
ATOM   2661 C  CA  . ALA B 1 54  ? -32.358 30.527  24.642  1.00 16.85  ? 54  ALA B CA  1 
ATOM   2662 C  C   . ALA B 1 54  ? -32.124 30.727  23.120  1.00 21.60  ? 54  ALA B C   1 
ATOM   2663 O  O   . ALA B 1 54  ? -32.967 30.438  22.309  1.00 24.21  ? 54  ALA B O   1 
ATOM   2664 C  CB  . ALA B 1 54  ? -31.867 29.177  25.135  1.00 23.35  ? 54  ALA B CB  1 
ATOM   2665 N  N   . THR B 1 55  ? -30.967 31.273  22.737  1.00 20.42  ? 55  THR B N   1 
ATOM   2666 C  CA  . THR B 1 55  ? -30.576 31.491  21.356  1.00 19.15  ? 55  THR B CA  1 
ATOM   2667 C  C   . THR B 1 55  ? -29.231 30.851  21.148  1.00 19.86  ? 55  THR B C   1 
ATOM   2668 O  O   . THR B 1 55  ? -28.179 31.468  21.419  1.00 20.93  ? 55  THR B O   1 
ATOM   2669 C  CB  . THR B 1 55  ? -30.311 32.963  20.991  1.00 27.12  ? 55  THR B CB  1 
ATOM   2670 O  OG1 . THR B 1 55  ? -31.565 33.636  21.026  1.00 25.72  ? 55  THR B OG1 1 
ATOM   2671 C  CG2 . THR B 1 55  ? -29.782 33.135  19.559  1.00 26.61  ? 55  THR B CG2 1 
ATOM   2672 N  N   . SER B 1 56  ? -29.344 29.595  20.760  1.00 19.93  ? 56  SER B N   1 
ATOM   2673 C  CA  . SER B 1 56  ? -28.151 28.926  20.357  1.00 17.94  ? 56  SER B CA  1 
ATOM   2674 C  C   . SER B 1 56  ? -27.875 29.590  19.027  1.00 16.61  ? 56  SER B C   1 
ATOM   2675 O  O   . SER B 1 56  ? -28.816 30.017  18.320  1.00 15.64  ? 56  SER B O   1 
ATOM   2676 C  CB  . SER B 1 56  ? -28.341 27.401  20.199  1.00 20.76  ? 56  SER B CB  1 
ATOM   2677 O  OG  . SER B 1 56  ? -28.784 27.049  18.854  1.00 23.43  ? 56  SER B OG  1 
ATOM   2678 N  N   . LEU B 1 57  ? -26.610 29.610  18.764  1.00 10.97  ? 57  LEU B N   1 
ATOM   2679 C  CA  . LEU B 1 57  ? -26.112 30.247  17.557  1.00 14.27  ? 57  LEU B CA  1 
ATOM   2680 C  C   . LEU B 1 57  ? -25.270 29.308  16.718  1.00 13.62  ? 57  LEU B C   1 
ATOM   2681 O  O   . LEU B 1 57  ? -25.206 29.431  15.492  1.00 13.52  ? 57  LEU B O   1 
ATOM   2682 C  CB  . LEU B 1 57  ? -25.215 31.402  17.930  1.00 16.31  ? 57  LEU B CB  1 
ATOM   2683 C  CG  . LEU B 1 57  ? -25.850 32.606  18.635  1.00 21.29  ? 57  LEU B CG  1 
ATOM   2684 C  CD1 . LEU B 1 57  ? -24.793 33.611  19.109  1.00 22.98  ? 57  LEU B CD1 1 
ATOM   2685 C  CD2 . LEU B 1 57  ? -26.867 33.288  17.707  1.00 21.99  ? 57  LEU B CD2 1 
ATOM   2686 N  N   B ARG B 1 58  ? -24.397 28.554  17.410  0.38 13.57  ? 58  ARG B N   1 
ATOM   2687 N  N   C ARG B 1 58  ? -24.347 28.626  17.436  0.62 13.75  ? 58  ARG B N   1 
ATOM   2688 C  CA  B ARG B 1 58  ? -23.145 28.059  16.816  0.38 13.33  ? 58  ARG B CA  1 
ATOM   2689 C  CA  C ARG B 1 58  ? -23.280 27.913  16.762  0.62 12.51  ? 58  ARG B CA  1 
ATOM   2690 C  C   B ARG B 1 58  ? -22.624 26.816  17.557  0.38 15.14  ? 58  ARG B C   1 
ATOM   2691 C  C   C ARG B 1 58  ? -22.924 26.623  17.481  0.62 11.56  ? 58  ARG B C   1 
ATOM   2692 O  O   B ARG B 1 58  ? -22.673 26.841  18.788  0.38 11.62  ? 58  ARG B O   1 
ATOM   2693 O  O   C ARG B 1 58  ? -23.162 26.530  18.682  0.62 12.00  ? 58  ARG B O   1 
ATOM   2694 C  CB  B ARG B 1 58  ? -22.151 29.211  16.583  0.38 14.74  ? 58  ARG B CB  1 
ATOM   2695 C  CB  C ARG B 1 58  ? -22.010 28.726  16.609  0.62 14.69  ? 58  ARG B CB  1 
ATOM   2696 C  CG  B ARG B 1 58  ? -20.776 28.899  15.995  0.38 12.14  ? 58  ARG B CG  1 
ATOM   2697 C  CG  C ARG B 1 58  ? -21.006 28.453  15.503  0.62 12.30  ? 58  ARG B CG  1 
ATOM   2698 C  CD  B ARG B 1 58  ? -19.873 30.009  15.324  0.38 12.98  ? 58  ARG B CD  1 
ATOM   2699 C  CD  C ARG B 1 58  ? -19.787 29.332  15.392  0.62 11.89  ? 58  ARG B CD  1 
ATOM   2700 N  NE  B ARG B 1 58  ? -19.099 29.583  14.136  0.38 13.11  ? 58  ARG B NE  1 
ATOM   2701 N  NE  C ARG B 1 58  ? -19.105 29.514  16.637  0.62 11.47  ? 58  ARG B NE  1 
ATOM   2702 C  CZ  B ARG B 1 58  ? -19.455 29.689  12.843  0.38 14.38  ? 58  ARG B CZ  1 
ATOM   2703 C  CZ  C ARG B 1 58  ? -17.811 29.843  16.661  0.62 13.29  ? 58  ARG B CZ  1 
ATOM   2704 N  NH1 B ARG B 1 58  ? -18.785 29.019  11.920  0.38 16.76  ? 58  ARG B NH1 1 
ATOM   2705 N  NH1 C ARG B 1 58  ? -17.119 30.152  15.562  0.62 10.93  ? 58  ARG B NH1 1 
ATOM   2706 N  NH2 B ARG B 1 58  ? -20.560 30.335  12.491  0.38 37.74  ? 58  ARG B NH2 1 
ATOM   2707 N  NH2 C ARG B 1 58  ? -17.164 29.920  17.821  0.62 12.92  ? 58  ARG B NH2 1 
ATOM   2708 N  N   . ILE B 1 59  ? -22.121 25.787  16.793  1.00 16.89  ? 59  ILE B N   1 
ATOM   2709 C  CA  . ILE B 1 59  ? -21.660 24.513  17.363  1.00 24.40  ? 59  ILE B CA  1 
ATOM   2710 C  C   . ILE B 1 59  ? -20.176 24.477  16.957  1.00 32.87  ? 59  ILE B C   1 
ATOM   2711 O  O   . ILE B 1 59  ? -19.828 24.700  15.749  1.00 22.22  ? 59  ILE B O   1 
ATOM   2712 C  CB  . ILE B 1 59  ? -22.410 23.281  16.911  1.00 13.99  ? 59  ILE B CB  1 
ATOM   2713 C  CG1 . ILE B 1 59  ? -21.849 22.122  17.782  1.00 21.96  ? 59  ILE B CG1 1 
ATOM   2714 C  CG2 . ILE B 1 59  ? -22.101 23.047  15.472  1.00 19.35  ? 59  ILE B CG2 1 
ATOM   2715 C  CD1 . ILE B 1 59  ? -22.721 20.926  17.868  1.00 23.06  ? 59  ILE B CD1 1 
ATOM   2716 N  N   . LEU B 1 60  ? -19.161 24.324  17.882  1.00 18.26  ? 60  LEU B N   1 
ATOM   2717 C  CA  . LEU B 1 60  ? -17.809 24.331  17.463  1.00 10.93  ? 60  LEU B CA  1 
ATOM   2718 C  C   . LEU B 1 60  ? -16.891 23.251  18.071  1.00 17.19  ? 60  LEU B C   1 
ATOM   2719 O  O   . LEU B 1 60  ? -17.128 22.961  19.241  1.00 13.01  ? 60  LEU B O   1 
ATOM   2720 C  CB  . LEU B 1 60  ? -17.299 25.723  17.847  1.00 17.03  ? 60  LEU B CB  1 
ATOM   2721 C  CG  . LEU B 1 60  ? -15.803 25.788  17.964  1.00 11.75  ? 60  LEU B CG  1 
ATOM   2722 C  CD1 . LEU B 1 60  ? -15.195 26.245  16.621  1.00 18.70  ? 60  LEU B CD1 1 
ATOM   2723 C  CD2 . LEU B 1 60  ? -15.399 26.820  19.030  1.00 19.97  ? 60  LEU B CD2 1 
ATOM   2724 N  N   . ASN B 1 61  ? -15.923 22.657  17.276  1.00 16.26  ? 61  ASN B N   1 
ATOM   2725 C  CA  . ASN B 1 61  ? -14.828 21.722  17.643  1.00 16.61  ? 61  ASN B CA  1 
ATOM   2726 C  C   . ASN B 1 61  ? -13.593 22.487  18.128  1.00 19.28  ? 61  ASN B C   1 
ATOM   2727 O  O   . ASN B 1 61  ? -12.934 23.020  17.278  1.00 22.17  ? 61  ASN B O   1 
ATOM   2728 C  CB  . ASN B 1 61  ? -14.399 20.641  16.586  1.00 19.13  ? 61  ASN B CB  1 
ATOM   2729 C  CG  . ASN B 1 61  ? -13.368 19.624  17.051  1.00 15.34  ? 61  ASN B CG  1 
ATOM   2730 O  OD1 . ASN B 1 61  ? -12.521 19.895  17.944  1.00 17.80  ? 61  ASN B OD1 1 
ATOM   2731 N  ND2 . ASN B 1 61  ? -13.388 18.427  16.472  1.00 15.29  ? 61  ASN B ND2 1 
ATOM   2732 N  N   . ASN B 1 62  ? -13.406 22.545  19.455  1.00 18.75  ? 62  ASN B N   1 
ATOM   2733 C  CA  . ASN B 1 62  ? -12.377 23.432  20.008  1.00 22.79  ? 62  ASN B CA  1 
ATOM   2734 C  C   . ASN B 1 62  ? -11.029 22.721  20.190  1.00 23.53  ? 62  ASN B C   1 
ATOM   2735 O  O   . ASN B 1 62  ? -10.037 23.271  20.779  1.00 31.52  ? 62  ASN B O   1 
ATOM   2736 C  CB  . ASN B 1 62  ? -12.817 24.065  21.339  1.00 22.26  ? 62  ASN B CB  1 
ATOM   2737 C  CG  . ASN B 1 62  ? -13.010 23.046  22.456  1.00 19.57  ? 62  ASN B CG  1 
ATOM   2738 O  OD1 . ASN B 1 62  ? -12.309 22.045  22.531  1.00 15.78  ? 62  ASN B OD1 1 
ATOM   2739 N  ND2 . ASN B 1 62  ? -13.995 23.283  23.301  1.00 20.04  ? 62  ASN B ND2 1 
ATOM   2740 N  N   . GLY B 1 63  ? -11.012 21.461  19.725  1.00 18.15  ? 63  GLY B N   1 
ATOM   2741 C  CA  . GLY B 1 63  ? -9.846  20.650  19.832  1.00 15.57  ? 63  GLY B CA  1 
ATOM   2742 C  C   . GLY B 1 63  ? -9.770  19.823  21.122  1.00 16.69  ? 63  GLY B C   1 
ATOM   2743 O  O   . GLY B 1 63  ? -8.888  18.973  21.248  1.00 13.11  ? 63  GLY B O   1 
ATOM   2744 N  N   . HIS B 1 64  ? -10.652 20.081  22.073  1.00 14.55  ? 64  HIS B N   1 
ATOM   2745 C  CA  . HIS B 1 64  ? -10.706 19.349  23.341  1.00 13.44  ? 64  HIS B CA  1 
ATOM   2746 C  C   . HIS B 1 64  ? -12.047 18.630  23.483  1.00 12.12  ? 64  HIS B C   1 
ATOM   2747 O  O   . HIS B 1 64  ? -12.076 17.465  23.962  1.00 13.75  ? 64  HIS B O   1 
ATOM   2748 C  CB  . HIS B 1 64  ? -10.426 20.206  24.556  1.00 14.80  ? 64  HIS B CB  1 
ATOM   2749 C  CG  . HIS B 1 64  ? -9.189  21.014  24.409  1.00 16.03  ? 64  HIS B CG  1 
ATOM   2750 N  ND1 . HIS B 1 64  ? -7.959  20.409  24.415  1.00 18.51  ? 64  HIS B ND1 1 
ATOM   2751 C  CD2 . HIS B 1 64  ? -8.991  22.320  24.150  1.00 16.23  ? 64  HIS B CD2 1 
ATOM   2752 C  CE1 . HIS B 1 64  ? -7.006  21.336  24.269  1.00 19.27  ? 64  HIS B CE1 1 
ATOM   2753 N  NE2 . HIS B 1 64  ? -7.618  22.498  24.115  1.00 19.76  ? 64  HIS B NE2 1 
ATOM   2754 N  N   . SER B 1 65  ? -13.105 19.323  23.066  1.00 12.40  ? 65  SER B N   1 
ATOM   2755 C  CA  . SER B 1 65  ? -14.448 18.844  23.076  1.00 10.49  ? 65  SER B CA  1 
ATOM   2756 C  C   . SER B 1 65  ? -15.143 19.584  21.939  1.00 10.36  ? 65  SER B C   1 
ATOM   2757 O  O   . SER B 1 65  ? -14.500 20.232  21.130  1.00 13.35  ? 65  SER B O   1 
ATOM   2758 C  CB  . SER B 1 65  ? -15.113 19.086  24.435  1.00 11.64  ? 65  SER B CB  1 
ATOM   2759 O  OG  . SER B 1 65  ? -16.371 18.411  24.340  1.00 14.19  ? 65  SER B OG  1 
ATOM   2760 N  N   . PHE B 1 66  ? -16.468 19.473  21.883  1.00 11.45  ? 66  PHE B N   1 
ATOM   2761 C  CA  . PHE B 1 66  ? -17.334 20.319  21.035  1.00 12.57  ? 66  PHE B CA  1 
ATOM   2762 C  C   . PHE B 1 66  ? -18.073 21.291  21.954  1.00 13.04  ? 66  PHE B C   1 
ATOM   2763 O  O   . PHE B 1 66  ? -18.200 20.940  23.156  1.00 12.78  ? 66  PHE B O   1 
ATOM   2764 C  CB  . PHE B 1 66  ? -18.147 19.610  19.974  1.00 12.74  ? 66  PHE B CB  1 
ATOM   2765 C  CG  . PHE B 1 66  ? -19.256 18.841  20.600  1.00 12.63  ? 66  PHE B CG  1 
ATOM   2766 C  CD1 . PHE B 1 66  ? -19.037 17.489  20.909  1.00 13.97  ? 66  PHE B CD1 1 
ATOM   2767 C  CD2 . PHE B 1 66  ? -20.518 19.384  20.811  1.00 14.04  ? 66  PHE B CD2 1 
ATOM   2768 C  CE1 . PHE B 1 66  ? -20.073 16.723  21.442  1.00 15.24  ? 66  PHE B CE1 1 
ATOM   2769 C  CE2 . PHE B 1 66  ? -21.526 18.604  21.361  1.00 16.50  ? 66  PHE B CE2 1 
ATOM   2770 C  CZ  . PHE B 1 66  ? -21.319 17.278  21.641  1.00 13.70  ? 66  PHE B CZ  1 
ATOM   2771 N  N   A GLN B 1 67  ? -18.784 22.386  21.503  0.50 9.59   ? 67  GLN B N   1 
ATOM   2772 N  N   B GLN B 1 67  ? -17.852 22.523  21.579  0.50 10.04  ? 67  GLN B N   1 
ATOM   2773 C  CA  A GLN B 1 67  ? -19.509 23.318  22.382  0.50 9.39   ? 67  GLN B CA  1 
ATOM   2774 C  CA  B GLN B 1 67  ? -18.558 23.529  22.300  0.50 10.64  ? 67  GLN B CA  1 
ATOM   2775 C  C   A GLN B 1 67  ? -20.651 23.968  21.577  0.50 6.85   ? 67  GLN B C   1 
ATOM   2776 C  C   B GLN B 1 67  ? -19.610 24.112  21.396  0.50 8.86   ? 67  GLN B C   1 
ATOM   2777 O  O   A GLN B 1 67  ? -20.452 24.443  20.450  0.50 8.09   ? 67  GLN B O   1 
ATOM   2778 O  O   B GLN B 1 67  ? -19.371 24.512  20.265  0.50 11.38  ? 67  GLN B O   1 
ATOM   2779 C  CB  A GLN B 1 67  ? -18.716 24.438  23.065  0.50 9.39   ? 67  GLN B CB  1 
ATOM   2780 C  CB  B GLN B 1 67  ? -17.646 24.618  22.836  0.50 8.71   ? 67  GLN B CB  1 
ATOM   2781 C  CG  A GLN B 1 67  ? -17.964 25.347  22.082  0.50 9.15   ? 67  GLN B CG  1 
ATOM   2782 C  CG  B GLN B 1 67  ? -16.822 25.289  21.757  0.50 8.62   ? 67  GLN B CG  1 
ATOM   2783 C  CD  A GLN B 1 67  ? -16.893 26.171  22.747  0.50 9.65   ? 67  GLN B CD  1 
ATOM   2784 C  CD  B GLN B 1 67  ? -15.693 26.136  22.321  0.50 11.40  ? 67  GLN B CD  1 
ATOM   2785 O  OE1 A GLN B 1 67  ? -16.083 25.673  23.519  0.50 11.11  ? 67  GLN B OE1 1 
ATOM   2786 O  OE1 B GLN B 1 67  ? -14.890 25.661  23.104  0.50 13.34  ? 67  GLN B OE1 1 
ATOM   2787 N  NE2 A GLN B 1 67  ? -16.868 27.441  22.392  0.50 11.41  ? 67  GLN B NE2 1 
ATOM   2788 N  NE2 B GLN B 1 67  ? -15.631 27.416  21.955  0.50 11.63  ? 67  GLN B NE2 1 
ATOM   2789 N  N   A VAL B 1 68  ? -21.845 24.034  22.189  0.50 7.01   ? 68  VAL B N   1 
ATOM   2790 N  N   B VAL B 1 68  ? -20.800 24.185  21.951  0.50 6.97   ? 68  VAL B N   1 
ATOM   2791 C  CA  A VAL B 1 68  ? -22.981 24.776  21.644  0.50 6.52   ? 68  VAL B CA  1 
ATOM   2792 C  CA  B VAL B 1 68  ? -21.872 24.937  21.355  0.50 7.68   ? 68  VAL B CA  1 
ATOM   2793 C  C   A VAL B 1 68  ? -23.110 26.095  22.372  0.50 6.32   ? 68  VAL B C   1 
ATOM   2794 C  C   B VAL B 1 68  ? -21.936 26.232  22.163  0.50 6.93   ? 68  VAL B C   1 
ATOM   2795 O  O   A VAL B 1 68  ? -23.239 26.127  23.575  0.50 7.22   ? 68  VAL B O   1 
ATOM   2796 O  O   B VAL B 1 68  ? -22.248 26.175  23.372  0.50 7.18   ? 68  VAL B O   1 
ATOM   2797 C  CB  A VAL B 1 68  ? -24.309 23.997  21.788  0.50 6.41   ? 68  VAL B CB  1 
ATOM   2798 C  CB  B VAL B 1 68  ? -23.193 24.131  21.427  0.50 7.32   ? 68  VAL B CB  1 
ATOM   2799 C  CG1 A VAL B 1 68  ? -25.533 24.823  21.399  0.50 9.08   ? 68  VAL B CG1 1 
ATOM   2800 C  CG1 B VAL B 1 68  ? -24.337 24.980  20.901  0.50 10.30  ? 68  VAL B CG1 1 
ATOM   2801 C  CG2 A VAL B 1 68  ? -24.302 22.710  20.977  0.50 6.58   ? 68  VAL B CG2 1 
ATOM   2802 C  CG2 B VAL B 1 68  ? -23.149 22.821  20.625  0.50 9.80   ? 68  VAL B CG2 1 
ATOM   2803 N  N   A GLU B 1 69  ? -22.948 27.147  21.582  0.50 6.99   ? 69  GLU B N   1 
ATOM   2804 N  N   B GLU B 1 69  ? -21.824 27.381  21.456  0.50 8.69   ? 69  GLU B N   1 
ATOM   2805 C  CA  A GLU B 1 69  ? -22.751 28.493  22.066  0.50 8.11   ? 69  GLU B CA  1 
ATOM   2806 C  CA  B GLU B 1 69  ? -21.935 28.775  22.045  0.50 9.72   ? 69  GLU B CA  1 
ATOM   2807 C  C   A GLU B 1 69  ? -24.080 29.139  21.965  0.50 7.02   ? 69  GLU B C   1 
ATOM   2808 C  C   B GLU B 1 69  ? -23.327 29.509  21.808  0.50 11.60  ? 69  GLU B C   1 
ATOM   2809 O  O   A GLU B 1 69  ? -24.561 29.275  20.823  0.50 6.95   ? 69  GLU B O   1 
ATOM   2810 O  O   B GLU B 1 69  ? -23.732 29.530  20.628  0.50 9.18   ? 69  GLU B O   1 
ATOM   2811 C  CB  A GLU B 1 69  ? -21.831 29.255  21.132  0.50 10.15  ? 69  GLU B CB  1 
ATOM   2812 C  CB  B GLU B 1 69  ? -20.650 29.493  21.555  0.50 11.33  ? 69  GLU B CB  1 
ATOM   2813 C  CG  A GLU B 1 69  ? -20.412 28.904  21.425  0.50 11.67  ? 69  GLU B CG  1 
ATOM   2814 C  CG  B GLU B 1 69  ? -19.353 28.722  21.819  0.50 11.92  ? 69  GLU B CG  1 
ATOM   2815 C  CD  A GLU B 1 69  ? -19.462 29.256  20.295  0.50 9.83   ? 69  GLU B CD  1 
ATOM   2816 C  CD  B GLU B 1 69  ? -18.122 29.576  21.540  0.50 12.00  ? 69  GLU B CD  1 
ATOM   2817 O  OE1 A GLU B 1 69  ? -19.937 29.854  19.335  0.50 11.03  ? 69  GLU B OE1 1 
ATOM   2818 O  OE1 B GLU B 1 69  ? -17.840 30.456  22.368  0.50 12.19  ? 69  GLU B OE1 1 
ATOM   2819 O  OE2 A GLU B 1 69  ? -18.355 28.755  20.320  0.50 11.66  ? 69  GLU B OE2 1 
ATOM   2820 O  OE2 B GLU B 1 69  ? -17.461 29.388  20.484  0.50 14.32  ? 69  GLU B OE2 1 
ATOM   2821 N  N   . PHE B 1 70  ? -24.048 30.088  22.844  1.00 13.80  ? 70  PHE B N   1 
ATOM   2822 C  CA  . PHE B 1 70  ? -25.291 30.866  22.891  1.00 14.07  ? 70  PHE B CA  1 
ATOM   2823 C  C   . PHE B 1 70  ? -25.098 32.380  22.820  1.00 17.99  ? 70  PHE B C   1 
ATOM   2824 O  O   . PHE B 1 70  ? -24.044 32.880  23.198  1.00 16.43  ? 70  PHE B O   1 
ATOM   2825 C  CB  . PHE B 1 70  ? -26.100 30.533  24.156  1.00 14.00  ? 70  PHE B CB  1 
ATOM   2826 C  CG  . PHE B 1 70  ? -26.635 29.124  24.148  1.00 15.73  ? 70  PHE B CG  1 
ATOM   2827 C  CD1 . PHE B 1 70  ? -25.790 28.053  24.403  1.00 14.55  ? 70  PHE B CD1 1 
ATOM   2828 C  CD2 . PHE B 1 70  ? -27.944 28.892  23.814  1.00 14.24  ? 70  PHE B CD2 1 
ATOM   2829 C  CE1 . PHE B 1 70  ? -26.270 26.742  24.339  1.00 16.86  ? 70  PHE B CE1 1 
ATOM   2830 C  CE2 . PHE B 1 70  ? -28.432 27.601  23.814  1.00 14.87  ? 70  PHE B CE2 1 
ATOM   2831 C  CZ  . PHE B 1 70  ? -27.600 26.515  24.003  1.00 16.83  ? 70  PHE B CZ  1 
ATOM   2832 N  N   . ASP B 1 71  ? -26.159 33.121  22.446  1.00 19.29  ? 71  ASP B N   1 
ATOM   2833 C  CA  . ASP B 1 71  ? -26.098 34.582  22.585  1.00 17.54  ? 71  ASP B CA  1 
ATOM   2834 C  C   . ASP B 1 71  ? -26.229 34.958  24.051  1.00 17.28  ? 71  ASP B C   1 
ATOM   2835 O  O   . ASP B 1 71  ? -27.305 34.772  24.583  1.00 23.42  ? 71  ASP B O   1 
ATOM   2836 C  CB  . ASP B 1 71  ? -27.248 35.172  21.742  1.00 20.50  ? 71  ASP B CB  1 
ATOM   2837 C  CG  . ASP B 1 71  ? -27.441 36.661  21.930  1.00 23.90  ? 71  ASP B CG  1 
ATOM   2838 O  OD1 . ASP B 1 71  ? -26.561 37.247  22.462  1.00 20.90  ? 71  ASP B OD1 1 
ATOM   2839 O  OD2 . ASP B 1 71  ? -28.493 37.217  21.578  1.00 26.54  ? 71  ASP B OD2 1 
ATOM   2840 N  N   . ASP B 1 72  ? -25.147 35.453  24.693  1.00 17.34  ? 72  ASP B N   1 
ATOM   2841 C  CA  . ASP B 1 72  ? -25.190 35.836  26.104  1.00 15.90  ? 72  ASP B CA  1 
ATOM   2842 C  C   . ASP B 1 72  ? -25.081 37.365  26.203  1.00 15.92  ? 72  ASP B C   1 
ATOM   2843 O  O   . ASP B 1 72  ? -24.558 37.897  27.181  1.00 18.21  ? 72  ASP B O   1 
ATOM   2844 C  CB  . ASP B 1 72  ? -24.010 35.222  26.881  1.00 16.63  ? 72  ASP B CB  1 
ATOM   2845 C  CG  . ASP B 1 72  ? -22.635 35.621  26.375  1.00 20.88  ? 72  ASP B CG  1 
ATOM   2846 O  OD1 . ASP B 1 72  ? -22.526 36.179  25.262  1.00 23.90  ? 72  ASP B OD1 1 
ATOM   2847 O  OD2 . ASP B 1 72  ? -21.659 35.272  27.092  1.00 21.13  ? 72  ASP B OD2 1 
ATOM   2848 N  N   . SER B 1 73  ? -25.555 38.051  25.147  1.00 18.54  ? 73  SER B N   1 
ATOM   2849 C  CA  . SER B 1 73  ? -25.512 39.517  25.123  1.00 19.36  ? 73  SER B CA  1 
ATOM   2850 C  C   . SER B 1 73  ? -26.722 40.170  25.806  1.00 22.20  ? 73  SER B C   1 
ATOM   2851 O  O   . SER B 1 73  ? -26.774 41.384  25.907  1.00 25.96  ? 73  SER B O   1 
ATOM   2852 C  CB  . SER B 1 73  ? -25.400 40.063  23.737  1.00 21.38  ? 73  SER B CB  1 
ATOM   2853 O  OG  . SER B 1 73  ? -26.661 39.945  23.101  1.00 21.49  ? 73  SER B OG  1 
ATOM   2854 N  N   . GLN B 1 74  ? -27.687 39.357  26.247  1.00 22.55  ? 74  GLN B N   1 
ATOM   2855 C  CA  . GLN B 1 74  ? -28.828 39.809  27.043  1.00 22.93  ? 74  GLN B CA  1 
ATOM   2856 C  C   . GLN B 1 74  ? -29.241 38.651  27.936  1.00 20.15  ? 74  GLN B C   1 
ATOM   2857 O  O   . GLN B 1 74  ? -28.834 37.518  27.659  1.00 19.65  ? 74  GLN B O   1 
ATOM   2858 C  CB  . GLN B 1 74  ? -30.078 39.981  26.185  1.00 30.23  ? 74  GLN B CB  1 
ATOM   2859 C  CG  . GLN B 1 74  ? -30.032 40.944  25.015  1.00 38.92  ? 74  GLN B CG  1 
ATOM   2860 C  CD  . GLN B 1 74  ? -31.389 40.898  24.351  1.00 36.66  ? 74  GLN B CD  1 
ATOM   2861 O  OE1 . GLN B 1 74  ? -32.446 41.075  24.996  1.00 44.02  ? 74  GLN B OE1 1 
ATOM   2862 N  NE2 . GLN B 1 74  ? -31.383 40.624  23.048  1.00 32.19  ? 74  GLN B NE2 1 
ATOM   2863 N  N   . ASP B 1 75  ? -30.106 38.904  28.939  1.00 21.92  ? 75  ASP B N   1 
ATOM   2864 C  CA  . ASP B 1 75  ? -30.711 37.849  29.757  1.00 22.24  ? 75  ASP B CA  1 
ATOM   2865 C  C   . ASP B 1 75  ? -31.713 37.145  28.847  1.00 24.41  ? 75  ASP B C   1 
ATOM   2866 O  O   . ASP B 1 75  ? -32.688 37.748  28.410  1.00 39.07  ? 75  ASP B O   1 
ATOM   2867 C  CB  . ASP B 1 75  ? -31.315 38.344  31.096  1.00 25.59  ? 75  ASP B CB  1 
ATOM   2868 C  CG  . ASP B 1 75  ? -30.324 38.894  32.144  1.00 23.91  ? 75  ASP B CG  1 
ATOM   2869 O  OD1 . ASP B 1 75  ? -29.097 38.666  32.009  1.00 29.15  ? 75  ASP B OD1 1 
ATOM   2870 O  OD2 . ASP B 1 75  ? -30.790 39.564  33.107  1.00 38.92  ? 75  ASP B OD2 1 
ATOM   2871 N  N   . LYS B 1 76  ? -31.363 35.955  28.426  1.00 19.67  ? 76  LYS B N   1 
ATOM   2872 C  CA  . LYS B 1 76  ? -32.266 35.070  27.740  1.00 20.94  ? 76  LYS B CA  1 
ATOM   2873 C  C   . LYS B 1 76  ? -32.356 33.775  28.543  1.00 27.99  ? 76  LYS B C   1 
ATOM   2874 O  O   . LYS B 1 76  ? -33.306 33.505  29.256  1.00 42.53  ? 76  LYS B O   1 
ATOM   2875 C  CB  . LYS B 1 76  ? -31.698 34.884  26.330  1.00 24.90  ? 76  LYS B CB  1 
ATOM   2876 C  CG  . LYS B 1 76  ? -32.002 36.070  25.430  1.00 25.70  ? 76  LYS B CG  1 
ATOM   2877 C  CD  . LYS B 1 76  ? -31.257 36.018  24.119  1.00 31.41  ? 76  LYS B CD  1 
ATOM   2878 C  CE  . LYS B 1 76  ? -31.840 36.985  23.101  1.00 28.46  ? 76  LYS B CE  1 
ATOM   2879 N  NZ  . LYS B 1 76  ? -31.592 36.490  21.738  1.00 26.29  ? 76  LYS B NZ  1 
ATOM   2880 N  N   . ALA B 1 77  ? -31.272 33.007  28.395  1.00 23.34  ? 77  ALA B N   1 
ATOM   2881 C  CA  . ALA B 1 77  ? -31.139 31.709  29.028  1.00 18.86  ? 77  ALA B CA  1 
ATOM   2882 C  C   . ALA B 1 77  ? -30.326 31.967  30.297  1.00 18.03  ? 77  ALA B C   1 
ATOM   2883 O  O   . ALA B 1 77  ? -29.136 32.318  30.259  1.00 18.93  ? 77  ALA B O   1 
ATOM   2884 C  CB  . ALA B 1 77  ? -30.432 30.790  28.084  1.00 22.13  ? 77  ALA B CB  1 
ATOM   2885 N  N   . VAL B 1 78  ? -30.973 31.780  31.457  1.00 15.84  ? 78  VAL B N   1 
ATOM   2886 C  CA  . VAL B 1 78  ? -30.331 32.118  32.716  1.00 15.10  ? 78  VAL B CA  1 
ATOM   2887 C  C   . VAL B 1 78  ? -30.568 31.037  33.771  1.00 12.50  ? 78  VAL B C   1 
ATOM   2888 O  O   . VAL B 1 78  ? -31.580 30.352  33.691  1.00 16.49  ? 78  VAL B O   1 
ATOM   2889 C  CB  . VAL B 1 78  ? -30.737 33.505  33.214  1.00 17.98  ? 78  VAL B CB  1 
ATOM   2890 C  CG1 . VAL B 1 78  ? -30.454 34.644  32.260  1.00 20.01  ? 78  VAL B CG1 1 
ATOM   2891 C  CG2 . VAL B 1 78  ? -32.130 33.536  33.657  1.00 19.67  ? 78  VAL B CG2 1 
ATOM   2892 N  N   . LEU B 1 79  ? -29.599 30.861  34.677  1.00 11.95  ? 79  LEU B N   1 
ATOM   2893 C  CA  . LEU B 1 79  ? -29.652 30.043  35.863  1.00 11.55  ? 79  LEU B CA  1 
ATOM   2894 C  C   . LEU B 1 79  ? -29.727 30.952  37.072  1.00 12.74  ? 79  LEU B C   1 
ATOM   2895 O  O   . LEU B 1 79  ? -28.884 31.845  37.189  1.00 13.38  ? 79  LEU B O   1 
ATOM   2896 C  CB  . LEU B 1 79  ? -28.431 29.096  35.840  1.00 12.78  ? 79  LEU B CB  1 
ATOM   2897 C  CG  . LEU B 1 79  ? -28.320 28.029  36.889  1.00 13.53  ? 79  LEU B CG  1 
ATOM   2898 C  CD1 . LEU B 1 79  ? -29.450 27.005  36.515  1.00 17.21  ? 79  LEU B CD1 1 
ATOM   2899 C  CD2 . LEU B 1 79  ? -26.954 27.351  36.773  1.00 12.33  ? 79  LEU B CD2 1 
ATOM   2900 N  N   . LYS B 1 80  ? -30.614 30.637  38.010  1.00 13.85  ? 80  LYS B N   1 
ATOM   2901 C  CA  . LYS B 1 80  ? -30.676 31.332  39.287  1.00 13.94  ? 80  LYS B CA  1 
ATOM   2902 C  C   . LYS B 1 80  ? -31.099 30.359  40.389  1.00 12.94  ? 80  LYS B C   1 
ATOM   2903 O  O   . LYS B 1 80  ? -31.373 29.190  40.105  1.00 16.45  ? 80  LYS B O   1 
ATOM   2904 C  CB  . LYS B 1 80  ? -31.638 32.534  39.253  1.00 19.18  ? 80  LYS B CB  1 
ATOM   2905 C  CG  . LYS B 1 80  ? -31.685 33.496  38.068  1.00 22.80  ? 80  LYS B CG  1 
ATOM   2906 C  CD  . LYS B 1 80  ? -33.069 34.183  37.985  1.00 31.86  ? 80  LYS B CD  1 
ATOM   2907 C  CE  . LYS B 1 80  ? -33.069 35.496  37.213  1.00 41.72  ? 80  LYS B CE  1 
ATOM   2908 N  NZ  . LYS B 1 80  ? -34.428 35.942  36.811  1.00 41.27  ? 80  LYS B NZ  1 
ATOM   2909 N  N   . GLY B 1 81  ? -31.275 30.887  41.578  1.00 14.56  ? 81  GLY B N   1 
ATOM   2910 C  CA  . GLY B 1 81  ? -31.679 30.150  42.747  1.00 15.98  ? 81  GLY B CA  1 
ATOM   2911 C  C   . GLY B 1 81  ? -30.710 29.040  43.068  1.00 14.82  ? 81  GLY B C   1 
ATOM   2912 O  O   . GLY B 1 81  ? -29.523 29.215  42.821  1.00 12.62  ? 81  GLY B O   1 
ATOM   2913 N  N   . GLY B 1 82  ? -31.205 27.937  43.623  1.00 18.79  ? 82  GLY B N   1 
ATOM   2914 C  CA  . GLY B 1 82  ? -30.282 26.910  44.078  1.00 21.24  ? 82  GLY B CA  1 
ATOM   2915 C  C   . GLY B 1 82  ? -29.336 27.510  45.124  1.00 19.54  ? 82  GLY B C   1 
ATOM   2916 O  O   . GLY B 1 82  ? -29.781 28.241  46.017  1.00 29.24  ? 82  GLY B O   1 
ATOM   2917 N  N   . PRO B 1 83  ? -28.017 27.302  44.975  1.00 16.40  ? 83  PRO B N   1 
ATOM   2918 C  CA  . PRO B 1 83  ? -27.072 27.943  45.887  1.00 14.60  ? 83  PRO B CA  1 
ATOM   2919 C  C   . PRO B 1 83  ? -26.649 29.355  45.474  1.00 13.85  ? 83  PRO B C   1 
ATOM   2920 O  O   . PRO B 1 83  ? -25.853 29.966  46.126  1.00 19.52  ? 83  PRO B O   1 
ATOM   2921 C  CB  . PRO B 1 83  ? -25.838 27.006  45.707  1.00 15.75  ? 83  PRO B CB  1 
ATOM   2922 C  CG  . PRO B 1 83  ? -25.920 26.664  44.248  1.00 12.92  ? 83  PRO B CG  1 
ATOM   2923 C  CD  . PRO B 1 83  ? -27.382 26.458  43.945  1.00 13.94  ? 83  PRO B CD  1 
ATOM   2924 N  N   . LEU B 1 84  ? -27.184 29.843  44.363  1.00 11.50  ? 84  LEU B N   1 
ATOM   2925 C  CA  . LEU B 1 84  ? -26.679 31.028  43.709  1.00 11.37  ? 84  LEU B CA  1 
ATOM   2926 C  C   . LEU B 1 84  ? -27.305 32.300  44.262  1.00 14.40  ? 84  LEU B C   1 
ATOM   2927 O  O   . LEU B 1 84  ? -28.496 32.317  44.560  1.00 16.17  ? 84  LEU B O   1 
ATOM   2928 C  CB  . LEU B 1 84  ? -26.914 30.977  42.215  1.00 11.00  ? 84  LEU B CB  1 
ATOM   2929 C  CG  . LEU B 1 84  ? -26.371 29.697  41.548  1.00 10.03  ? 84  LEU B CG  1 
ATOM   2930 C  CD1 . LEU B 1 84  ? -26.785 29.693  40.079  1.00 12.20  ? 84  LEU B CD1 1 
ATOM   2931 C  CD2 . LEU B 1 84  ? -24.787 29.698  41.679  1.00 11.07  ? 84  LEU B CD2 1 
ATOM   2932 N  N   . ASP B 1 85  ? -26.505 33.379  44.276  1.00 14.78  ? 85  ASP B N   1 
ATOM   2933 C  CA  . ASP B 1 85  ? -26.980 34.743  44.509  1.00 17.55  ? 85  ASP B CA  1 
ATOM   2934 C  C   . ASP B 1 85  ? -27.000 35.341  43.097  1.00 20.72  ? 85  ASP B C   1 
ATOM   2935 O  O   . ASP B 1 85  ? -26.015 35.209  42.372  1.00 25.18  ? 85  ASP B O   1 
ATOM   2936 C  CB  . ASP B 1 85  ? -25.984 35.484  45.426  1.00 31.90  ? 85  ASP B CB  1 
ATOM   2937 C  CG  . ASP B 1 85  ? -26.027 35.008  46.876  1.00 35.62  ? 85  ASP B CG  1 
ATOM   2938 O  OD1 . ASP B 1 85  ? -26.944 34.201  47.190  1.00 51.37  ? 85  ASP B OD1 1 
ATOM   2939 O  OD2 . ASP B 1 85  ? -25.177 35.461  47.693  1.00 41.00  ? 85  ASP B OD2 1 
ATOM   2940 N  N   . GLY B 1 86  ? -28.080 35.993  42.665  1.00 23.31  ? 86  GLY B N   1 
ATOM   2941 C  CA  . GLY B 1 86  ? -28.038 36.728  41.397  1.00 26.17  ? 86  GLY B CA  1 
ATOM   2942 C  C   . GLY B 1 86  ? -28.211 35.824  40.175  1.00 18.38  ? 86  GLY B C   1 
ATOM   2943 O  O   . GLY B 1 86  ? -28.705 34.706  40.300  1.00 22.05  ? 86  GLY B O   1 
ATOM   2944 N  N   . THR B 1 87  ? -27.869 36.332  38.993  1.00 13.95  ? 87  THR B N   1 
ATOM   2945 C  CA  . THR B 1 87  ? -28.369 35.773  37.731  1.00 12.51  ? 87  THR B CA  1 
ATOM   2946 C  C   . THR B 1 87  ? -27.131 35.362  36.944  1.00 11.24  ? 87  THR B C   1 
ATOM   2947 O  O   . THR B 1 87  ? -26.191 36.140  36.862  1.00 11.87  ? 87  THR B O   1 
ATOM   2948 C  CB  . THR B 1 87  ? -29.126 36.854  36.973  1.00 19.33  ? 87  THR B CB  1 
ATOM   2949 O  OG1 . THR B 1 87  ? -30.356 37.069  37.698  1.00 24.35  ? 87  THR B OG1 1 
ATOM   2950 C  CG2 . THR B 1 87  ? -29.591 36.402  35.593  1.00 22.76  ? 87  THR B CG2 1 
ATOM   2951 N  N   . TYR B 1 88  ? -27.188 34.148  36.385  1.00 10.72  ? 88  TYR B N   1 
ATOM   2952 C  CA  . TYR B 1 88  ? -26.053 33.650  35.616  1.00 10.59  ? 88  TYR B CA  1 
ATOM   2953 C  C   . TYR B 1 88  ? -26.512 33.352  34.185  1.00 10.54  ? 88  TYR B C   1 
ATOM   2954 O  O   . TYR B 1 88  ? -27.485 32.590  33.977  1.00 13.99  ? 88  TYR B O   1 
ATOM   2955 C  CB  . TYR B 1 88  ? -25.484 32.403  36.263  1.00 10.79  ? 88  TYR B CB  1 
ATOM   2956 C  CG  . TYR B 1 88  ? -24.713 32.604  37.555  1.00 9.04   ? 88  TYR B CG  1 
ATOM   2957 C  CD1 . TYR B 1 88  ? -25.384 32.990  38.719  1.00 9.30   ? 88  TYR B CD1 1 
ATOM   2958 C  CD2 . TYR B 1 88  ? -23.345 32.369  37.613  1.00 8.07   ? 88  TYR B CD2 1 
ATOM   2959 C  CE1 . TYR B 1 88  ? -24.698 33.172  39.915  1.00 9.09   ? 88  TYR B CE1 1 
ATOM   2960 C  CE2 . TYR B 1 88  ? -22.644 32.565  38.802  1.00 7.98   ? 88  TYR B CE2 1 
ATOM   2961 C  CZ  . TYR B 1 88  ? -23.298 32.943  39.939  1.00 8.10   ? 88  TYR B CZ  1 
ATOM   2962 O  OH  . TYR B 1 88  ? -22.638 33.072  41.122  1.00 9.14   ? 88  TYR B OH  1 
ATOM   2963 N  N   . ARG B 1 89  ? -25.856 33.915  33.181  1.00 9.84   ? 89  ARG B N   1 
ATOM   2964 C  CA  . ARG B 1 89  ? -26.271 33.767  31.796  1.00 11.76  ? 89  ARG B CA  1 
ATOM   2965 C  C   . ARG B 1 89  ? -25.573 32.564  31.142  1.00 8.65   ? 89  ARG B C   1 
ATOM   2966 O  O   . ARG B 1 89  ? -24.379 32.382  31.304  1.00 8.64   ? 89  ARG B O   1 
ATOM   2967 C  CB  . ARG B 1 89  ? -25.873 34.943  30.892  1.00 14.04  ? 89  ARG B CB  1 
ATOM   2968 C  CG  . ARG B 1 89  ? -26.472 36.317  31.149  1.00 16.53  ? 89  ARG B CG  1 
ATOM   2969 C  CD  . ARG B 1 89  ? -26.270 37.258  29.976  1.00 19.90  ? 89  ARG B CD  1 
ATOM   2970 N  NE  . ARG B 1 89  ? -26.854 38.559  30.251  1.00 21.37  ? 89  ARG B NE  1 
ATOM   2971 C  CZ  . ARG B 1 89  ? -26.386 39.715  29.817  1.00 23.79  ? 89  ARG B CZ  1 
ATOM   2972 N  NH1 . ARG B 1 89  ? -25.270 39.779  29.102  1.00 21.72  ? 89  ARG B NH1 1 
ATOM   2973 N  NH2 . ARG B 1 89  ? -26.998 40.829  30.197  1.00 27.46  ? 89  ARG B NH2 1 
ATOM   2974 N  N   . LEU B 1 90  ? -26.361 31.730  30.436  1.00 9.70   ? 90  LEU B N   1 
ATOM   2975 C  CA  . LEU B 1 90  ? -25.831 30.590  29.715  1.00 10.38  ? 90  LEU B CA  1 
ATOM   2976 C  C   . LEU B 1 90  ? -24.965 31.074  28.555  1.00 11.91  ? 90  LEU B C   1 
ATOM   2977 O  O   . LEU B 1 90  ? -25.446 31.827  27.708  1.00 12.88  ? 90  LEU B O   1 
ATOM   2978 C  CB  . LEU B 1 90  ? -27.010 29.713  29.179  1.00 12.31  ? 90  LEU B CB  1 
ATOM   2979 C  CG  . LEU B 1 90  ? -26.545 28.573  28.242  1.00 12.97  ? 90  LEU B CG  1 
ATOM   2980 C  CD1 . LEU B 1 90  ? -25.675 27.520  28.967  1.00 14.28  ? 90  LEU B CD1 1 
ATOM   2981 C  CD2 . LEU B 1 90  ? -27.736 27.938  27.531  1.00 15.26  ? 90  LEU B CD2 1 
ATOM   2982 N  N   . LEU B 1 91  ? -23.696 30.631  28.550  1.00 10.04  ? 91  LEU B N   1 
ATOM   2983 C  CA  . LEU B 1 91  ? -22.731 30.916  27.488  1.00 11.30  ? 91  LEU B CA  1 
ATOM   2984 C  C   . LEU B 1 91  ? -22.611 29.758  26.519  1.00 10.89  ? 91  LEU B C   1 
ATOM   2985 O  O   . LEU B 1 91  ? -22.543 29.967  25.301  1.00 10.92  ? 91  LEU B O   1 
ATOM   2986 C  CB  . LEU B 1 91  ? -21.370 31.234  28.155  1.00 12.94  ? 91  LEU B CB  1 
ATOM   2987 C  CG  . LEU B 1 91  ? -20.166 31.351  27.211  1.00 13.17  ? 91  LEU B CG  1 
ATOM   2988 C  CD1 . LEU B 1 91  ? -20.289 32.477  26.170  1.00 22.37  ? 91  LEU B CD1 1 
ATOM   2989 C  CD2 . LEU B 1 91  ? -18.967 31.681  28.024  1.00 17.35  ? 91  LEU B CD2 1 
ATOM   2990 N  N   . GLN B 1 92  ? -22.456 28.542  27.056  1.00 11.13  ? 92  GLN B N   1 
ATOM   2991 C  CA  . GLN B 1 92  ? -22.179 27.437  26.179  1.00 11.80  ? 92  GLN B CA  1 
ATOM   2992 C  C   . GLN B 1 92  ? -22.380 26.136  26.922  1.00 8.33   ? 92  GLN B C   1 
ATOM   2993 O  O   . GLN B 1 92  ? -22.421 26.117  28.138  1.00 9.97   ? 92  GLN B O   1 
ATOM   2994 C  CB  . GLN B 1 92  ? -20.738 27.456  25.661  1.00 11.93  ? 92  GLN B CB  1 
ATOM   2995 C  CG  . GLN B 1 92  ? -19.798 27.360  26.847  1.00 12.83  ? 92  GLN B CG  1 
ATOM   2996 C  CD  . GLN B 1 92  ? -18.774 26.295  26.607  1.00 16.37  ? 92  GLN B CD  1 
ATOM   2997 O  OE1 . GLN B 1 92  ? -19.030 25.124  26.875  1.00 23.68  ? 92  GLN B OE1 1 
ATOM   2998 N  NE2 . GLN B 1 92  ? -17.670 26.674  25.946  1.00 23.34  ? 92  GLN B NE2 1 
ATOM   2999 N  N   . PHE B 1 93  ? -22.569 25.062  26.173  1.00 10.19  ? 93  PHE B N   1 
ATOM   3000 C  CA  . PHE B 1 93  ? -22.382 23.747  26.738  1.00 10.64  ? 93  PHE B CA  1 
ATOM   3001 C  C   . PHE B 1 93  ? -21.420 22.885  25.961  1.00 10.86  ? 93  PHE B C   1 
ATOM   3002 O  O   . PHE B 1 93  ? -21.155 23.103  24.781  1.00 11.24  ? 93  PHE B O   1 
ATOM   3003 C  CB  . PHE B 1 93  ? -23.721 23.008  26.948  1.00 10.83  ? 93  PHE B CB  1 
ATOM   3004 C  CG  . PHE B 1 93  ? -24.442 22.565  25.690  1.00 11.42  ? 93  PHE B CG  1 
ATOM   3005 C  CD1 . PHE B 1 93  ? -24.003 21.498  24.948  1.00 12.88  ? 93  PHE B CD1 1 
ATOM   3006 C  CD2 . PHE B 1 93  ? -25.569 23.253  25.278  1.00 14.09  ? 93  PHE B CD2 1 
ATOM   3007 C  CE1 . PHE B 1 93  ? -24.769 21.051  23.872  1.00 14.00  ? 93  PHE B CE1 1 
ATOM   3008 C  CE2 . PHE B 1 93  ? -26.292 22.846  24.166  1.00 16.15  ? 93  PHE B CE2 1 
ATOM   3009 C  CZ  . PHE B 1 93  ? -25.893 21.732  23.455  1.00 17.32  ? 93  PHE B CZ  1 
ATOM   3010 N  N   . HIS B 1 94  ? -20.829 21.924  26.688  1.00 9.38   ? 94  HIS B N   1 
ATOM   3011 C  CA  . HIS B 1 94  ? -19.995 20.939  26.057  1.00 8.24   ? 94  HIS B CA  1 
ATOM   3012 C  C   . HIS B 1 94  ? -20.065 19.671  26.878  1.00 6.86   ? 94  HIS B C   1 
ATOM   3013 O  O   . HIS B 1 94  ? -20.722 19.595  27.889  1.00 7.66   ? 94  HIS B O   1 
ATOM   3014 C  CB  . HIS B 1 94  ? -18.503 21.489  26.046  1.00 9.61   ? 94  HIS B CB  1 
ATOM   3015 C  CG  . HIS B 1 94  ? -18.020 21.751  27.430  1.00 8.15   ? 94  HIS B CG  1 
ATOM   3016 N  ND1 . HIS B 1 94  ? -18.177 22.974  28.058  1.00 7.78   ? 94  HIS B ND1 1 
ATOM   3017 C  CD2 . HIS B 1 94  ? -17.491 20.891  28.315  1.00 7.98   ? 94  HIS B CD2 1 
ATOM   3018 C  CE1 . HIS B 1 94  ? -17.702 22.859  29.303  1.00 7.41   ? 94  HIS B CE1 1 
ATOM   3019 N  NE2 . HIS B 1 94  ? -17.290 21.582  29.493  1.00 6.20   ? 94  HIS B NE2 1 
ATOM   3020 N  N   . PHE B 1 95  ? -19.335 18.658  26.385  1.00 8.03   ? 95  PHE B N   1 
ATOM   3021 C  CA  . PHE B 1 95  ? -19.365 17.359  27.071  1.00 7.79   ? 95  PHE B CA  1 
ATOM   3022 C  C   . PHE B 1 95  ? -17.957 16.831  27.292  1.00 6.05   ? 95  PHE B C   1 
ATOM   3023 O  O   . PHE B 1 95  ? -17.005 17.264  26.666  1.00 7.74   ? 95  PHE B O   1 
ATOM   3024 C  CB  . PHE B 1 95  ? -20.099 16.321  26.202  1.00 7.91   ? 95  PHE B CB  1 
ATOM   3025 C  CG  . PHE B 1 95  ? -21.562 16.586  25.946  1.00 7.58   ? 95  PHE B CG  1 
ATOM   3026 C  CD1 . PHE B 1 95  ? -21.913 17.445  24.961  1.00 8.68   ? 95  PHE B CD1 1 
ATOM   3027 C  CD2 . PHE B 1 95  ? -22.555 15.854  26.614  1.00 9.00   ? 95  PHE B CD2 1 
ATOM   3028 C  CE1 . PHE B 1 95  ? -23.216 17.661  24.584  1.00 9.80   ? 95  PHE B CE1 1 
ATOM   3029 C  CE2 . PHE B 1 95  ? -23.885 16.066  26.268  1.00 9.00   ? 95  PHE B CE2 1 
ATOM   3030 C  CZ  . PHE B 1 95  ? -24.211 17.012  25.294  1.00 9.16   ? 95  PHE B CZ  1 
ATOM   3031 N  N   . HIS B 1 96  ? -17.822 15.898  28.225  1.00 7.29   ? 96  HIS B N   1 
ATOM   3032 C  CA  . HIS B 1 96  ? -16.661 15.072  28.415  1.00 7.32   ? 96  HIS B CA  1 
ATOM   3033 C  C   . HIS B 1 96  ? -17.099 13.635  28.319  1.00 6.13   ? 96  HIS B C   1 
ATOM   3034 O  O   . HIS B 1 96  ? -18.189 13.304  28.782  1.00 6.55   ? 96  HIS B O   1 
ATOM   3035 C  CB  . HIS B 1 96  ? -16.061 15.350  29.813  1.00 7.19   ? 96  HIS B CB  1 
ATOM   3036 C  CG  . HIS B 1 96  ? -15.760 16.755  30.117  1.00 6.91   ? 96  HIS B CG  1 
ATOM   3037 N  ND1 . HIS B 1 96  ? -14.498 17.293  29.914  1.00 7.03   ? 96  HIS B ND1 1 
ATOM   3038 C  CD2 . HIS B 1 96  ? -16.559 17.757  30.492  1.00 6.90   ? 96  HIS B CD2 1 
ATOM   3039 C  CE1 . HIS B 1 96  ? -14.595 18.581  30.241  1.00 5.97   ? 96  HIS B CE1 1 
ATOM   3040 N  NE2 . HIS B 1 96  ? -15.802 18.891  30.577  1.00 5.43   ? 96  HIS B NE2 1 
ATOM   3041 N  N   . TRP B 1 97  ? -16.321 12.768  27.681  1.00 6.70   ? 97  TRP B N   1 
ATOM   3042 C  CA  . TRP B 1 97  ? -16.738 11.391  27.494  1.00 6.86   ? 97  TRP B CA  1 
ATOM   3043 C  C   . TRP B 1 97  ? -15.527 10.483  27.354  1.00 6.26   ? 97  TRP B C   1 
ATOM   3044 O  O   . TRP B 1 97  ? -14.349 10.952  27.268  1.00 7.25   ? 97  TRP B O   1 
ATOM   3045 C  CB  . TRP B 1 97  ? -17.624 11.247  26.230  1.00 7.04   ? 97  TRP B CB  1 
ATOM   3046 C  CG  . TRP B 1 97  ? -16.949 11.609  24.944  1.00 7.40   ? 97  TRP B CG  1 
ATOM   3047 C  CD1 . TRP B 1 97  ? -16.201 10.776  24.140  1.00 8.39   ? 97  TRP B CD1 1 
ATOM   3048 C  CD2 . TRP B 1 97  ? -16.939 12.894  24.318  1.00 8.00   ? 97  TRP B CD2 1 
ATOM   3049 N  NE1 . TRP B 1 97  ? -15.819 11.463  23.045  1.00 9.92   ? 97  TRP B NE1 1 
ATOM   3050 C  CE2 . TRP B 1 97  ? -16.240 12.767  23.136  1.00 7.89   ? 97  TRP B CE2 1 
ATOM   3051 C  CE3 . TRP B 1 97  ? -17.477 14.143  24.684  1.00 7.90   ? 97  TRP B CE3 1 
ATOM   3052 C  CZ2 . TRP B 1 97  ? -16.067 13.838  22.273  1.00 10.15  ? 97  TRP B CZ2 1 
ATOM   3053 C  CZ3 . TRP B 1 97  ? -17.280 15.209  23.812  1.00 8.75   ? 97  TRP B CZ3 1 
ATOM   3054 C  CH2 . TRP B 1 97  ? -16.562 15.064  22.626  1.00 10.43  ? 97  TRP B CH2 1 
ATOM   3055 N  N   . GLY B 1 98  ? -15.828 9.200   27.379  1.00 6.62   ? 98  GLY B N   1 
ATOM   3056 C  CA  . GLY B 1 98  ? -14.827 8.149   27.500  1.00 8.22   ? 98  GLY B CA  1 
ATOM   3057 C  C   . GLY B 1 98  ? -14.568 7.420   26.178  1.00 7.28   ? 98  GLY B C   1 
ATOM   3058 O  O   . GLY B 1 98  ? -15.302 7.559   25.227  1.00 7.87   ? 98  GLY B O   1 
ATOM   3059 N  N   . SER B 1 99  ? -13.526 6.597   26.174  1.00 7.89   ? 99  SER B N   1 
ATOM   3060 C  CA  . SER B 1 99  ? -13.332 5.593   25.127  1.00 8.55   ? 99  SER B CA  1 
ATOM   3061 C  C   . SER B 1 99  ? -14.259 4.378   25.268  1.00 8.44   ? 99  SER B C   1 
ATOM   3062 O  O   . SER B 1 99  ? -14.474 3.649   24.292  1.00 10.66  ? 99  SER B O   1 
ATOM   3063 C  CB  . SER B 1 99  ? -11.892 5.194   25.083  1.00 9.35   ? 99  SER B CB  1 
ATOM   3064 O  OG  . SER B 1 99  ? -11.404 4.810   26.329  1.00 10.60  ? 99  SER B OG  1 
ATOM   3065 N  N   . LEU B 1 100 ? -14.718 4.177   26.479  1.00 8.93   ? 100 LEU B N   1 
ATOM   3066 C  CA  . LEU B 1 100 ? -15.576 3.054   26.842  1.00 10.39  ? 100 LEU B CA  1 
ATOM   3067 C  C   . LEU B 1 100 ? -16.670 3.567   27.723  1.00 8.47   ? 100 LEU B C   1 
ATOM   3068 O  O   . LEU B 1 100 ? -16.480 4.603   28.348  1.00 9.59   ? 100 LEU B O   1 
ATOM   3069 C  CB  . LEU B 1 100 ? -14.792 2.019   27.646  1.00 14.92  ? 100 LEU B CB  1 
ATOM   3070 C  CG  . LEU B 1 100 ? -13.476 1.611   27.004  1.00 15.66  ? 100 LEU B CG  1 
ATOM   3071 C  CD1 . LEU B 1 100 ? -12.580 0.905   28.000  1.00 20.26  ? 100 LEU B CD1 1 
ATOM   3072 C  CD2 . LEU B 1 100 ? -13.906 0.641   25.945  1.00 19.70  ? 100 LEU B CD2 1 
ATOM   3073 N  N   . ASP B 1 101 ? -17.759 2.832   27.812  1.00 8.23   ? 101 ASP B N   1 
ATOM   3074 C  CA  . ASP B 1 101 ? -18.884 3.330   28.564  1.00 9.64   ? 101 ASP B CA  1 
ATOM   3075 C  C   . ASP B 1 101 ? -18.665 3.441   30.080  1.00 9.10   ? 101 ASP B C   1 
ATOM   3076 O  O   . ASP B 1 101 ? -19.392 4.212   30.727  1.00 11.96  ? 101 ASP B O   1 
ATOM   3077 C  CB  . ASP B 1 101 ? -20.051 2.406   28.335  1.00 10.54  ? 101 ASP B CB  1 
ATOM   3078 C  CG  . ASP B 1 101 ? -20.611 2.363   26.936  1.00 12.81  ? 101 ASP B CG  1 
ATOM   3079 O  OD1 . ASP B 1 101 ? -20.269 3.230   26.087  1.00 12.78  ? 101 ASP B OD1 1 
ATOM   3080 O  OD2 . ASP B 1 101 ? -21.449 1.460   26.695  1.00 19.36  ? 101 ASP B OD2 1 
ATOM   3081 N  N   . GLY B 1 102 ? -17.635 2.756   30.612  1.00 9.76   ? 102 GLY B N   1 
ATOM   3082 C  CA  . GLY B 1 102 ? -17.320 2.817   32.038  1.00 10.59  ? 102 GLY B CA  1 
ATOM   3083 C  C   . GLY B 1 102 ? -16.474 3.991   32.509  1.00 8.79   ? 102 GLY B C   1 
ATOM   3084 O  O   . GLY B 1 102 ? -16.063 3.977   33.700  1.00 10.03  ? 102 GLY B O   1 
ATOM   3085 N  N   A GLN B 1 103 ? -16.107 4.913   31.599  0.50 6.85   ? 103 GLN B N   1 
ATOM   3086 N  N   B GLN B 1 103 ? -16.469 5.071   31.742  0.50 9.71   ? 103 GLN B N   1 
ATOM   3087 C  CA  A GLN B 1 103 ? -15.395 6.114   31.960  0.50 7.43   ? 103 GLN B CA  1 
ATOM   3088 C  CA  B GLN B 1 103 ? -15.624 6.177   32.119  0.50 8.83   ? 103 GLN B CA  1 
ATOM   3089 C  C   A GLN B 1 103 ? -15.925 7.242   31.096  0.50 6.87   ? 103 GLN B C   1 
ATOM   3090 C  C   B GLN B 1 103 ? -15.895 7.237   31.090  0.50 7.82   ? 103 GLN B C   1 
ATOM   3091 O  O   A GLN B 1 103 ? -16.534 7.034   30.036  0.50 5.86   ? 103 GLN B O   1 
ATOM   3092 O  O   B GLN B 1 103 ? -16.232 6.895   29.925  0.50 11.83  ? 103 GLN B O   1 
ATOM   3093 C  CB  A GLN B 1 103 ? -13.869 5.920   31.889  0.50 8.53   ? 103 GLN B CB  1 
ATOM   3094 C  CB  B GLN B 1 103 ? -14.149 5.759   32.128  0.50 10.05  ? 103 GLN B CB  1 
ATOM   3095 C  CG  A GLN B 1 103 ? -13.395 5.621   30.464  0.50 8.00   ? 103 GLN B CG  1 
ATOM   3096 C  CG  B GLN B 1 103 ? -13.614 5.395   30.747  0.50 12.25  ? 103 GLN B CG  1 
ATOM   3097 C  CD  A GLN B 1 103 ? -12.143 4.803   30.396  0.50 11.66  ? 103 GLN B CD  1 
ATOM   3098 C  CD  B GLN B 1 103 ? -12.128 5.118   30.767  0.50 17.30  ? 103 GLN B CD  1 
ATOM   3099 O  OE1 A GLN B 1 103 ? -12.122 3.697   30.919  0.50 14.36  ? 103 GLN B OE1 1 
ATOM   3100 O  OE1 B GLN B 1 103 ? -11.537 4.758   31.794  0.50 19.78  ? 103 GLN B OE1 1 
ATOM   3101 N  NE2 A GLN B 1 103 ? -11.062 5.416   29.877  0.50 11.47  ? 103 GLN B NE2 1 
ATOM   3102 N  NE2 B GLN B 1 103 ? -11.466 5.370   29.643  0.50 15.94  ? 103 GLN B NE2 1 
ATOM   3103 N  N   . GLY B 1 104 ? -15.607 8.486   31.532  1.00 7.32   ? 104 GLY B N   1 
ATOM   3104 C  CA  . GLY B 1 104 ? -15.888 9.642   30.719  1.00 7.12   ? 104 GLY B CA  1 
ATOM   3105 C  C   . GLY B 1 104 ? -16.357 10.808  31.529  1.00 6.33   ? 104 GLY B C   1 
ATOM   3106 O  O   . GLY B 1 104 ? -16.138 11.951  31.181  1.00 7.42   ? 104 GLY B O   1 
ATOM   3107 N  N   . SER B 1 105 ? -17.101 10.578  32.628  1.00 6.92   ? 105 SER B N   1 
ATOM   3108 C  CA  . SER B 1 105 ? -17.503 11.672  33.484  1.00 7.09   ? 105 SER B CA  1 
ATOM   3109 C  C   . SER B 1 105 ? -16.302 12.217  34.255  1.00 6.06   ? 105 SER B C   1 
ATOM   3110 O  O   . SER B 1 105 ? -15.244 11.566  34.463  1.00 6.58   ? 105 SER B O   1 
ATOM   3111 C  CB  . SER B 1 105 ? -18.653 11.278  34.426  1.00 7.93   ? 105 SER B CB  1 
ATOM   3112 O  OG  . SER B 1 105 ? -18.224 10.358  35.412  1.00 7.13   ? 105 SER B OG  1 
ATOM   3113 N  N   . GLU B 1 106 ? -16.457 13.462  34.685  1.00 6.16   ? 106 GLU B N   1 
ATOM   3114 C  CA  . GLU B 1 106 ? -15.425 14.170  35.467  1.00 6.58   ? 106 GLU B CA  1 
ATOM   3115 C  C   . GLU B 1 106 ? -15.689 14.039  36.935  1.00 5.82   ? 106 GLU B C   1 
ATOM   3116 O  O   . GLU B 1 106 ? -14.982 13.425  37.727  1.00 6.65   ? 106 GLU B O   1 
ATOM   3117 C  CB  . GLU B 1 106 ? -15.401 15.646  35.017  1.00 6.26   ? 106 GLU B CB  1 
ATOM   3118 C  CG  . GLU B 1 106 ? -14.883 15.766  33.574  1.00 7.08   ? 106 GLU B CG  1 
ATOM   3119 C  CD  . GLU B 1 106 ? -14.240 17.087  33.296  1.00 7.22   ? 106 GLU B CD  1 
ATOM   3120 O  OE1 . GLU B 1 106 ? -14.826 18.121  33.547  1.00 7.20   ? 106 GLU B OE1 1 
ATOM   3121 O  OE2 . GLU B 1 106 ? -13.072 17.007  32.793  1.00 7.61   ? 106 GLU B OE2 1 
ATOM   3122 N  N   . HIS B 1 107 ? -16.940 14.445  37.364  1.00 6.26   ? 107 HIS B N   1 
ATOM   3123 C  CA  . HIS B 1 107 ? -17.395 14.069  38.701  1.00 5.71   ? 107 HIS B CA  1 
ATOM   3124 C  C   . HIS B 1 107 ? -17.694 12.587  38.697  1.00 6.25   ? 107 HIS B C   1 
ATOM   3125 O  O   . HIS B 1 107 ? -18.051 11.974  37.670  1.00 6.26   ? 107 HIS B O   1 
ATOM   3126 C  CB  . HIS B 1 107 ? -18.733 14.828  39.090  1.00 6.82   ? 107 HIS B CB  1 
ATOM   3127 C  CG  . HIS B 1 107 ? -18.357 16.309  39.191  1.00 6.16   ? 107 HIS B CG  1 
ATOM   3128 N  ND1 . HIS B 1 107 ? -18.390 17.205  38.146  1.00 5.93   ? 107 HIS B ND1 1 
ATOM   3129 C  CD2 . HIS B 1 107 ? -17.874 17.067  40.269  1.00 6.34   ? 107 HIS B CD2 1 
ATOM   3130 C  CE1 . HIS B 1 107 ? -17.961 18.434  38.570  1.00 6.11   ? 107 HIS B CE1 1 
ATOM   3131 N  NE2 . HIS B 1 107 ? -17.626 18.367  39.850  1.00 6.09   ? 107 HIS B NE2 1 
ATOM   3132 N  N   . THR B 1 108 ? -17.563 12.019  39.893  1.00 6.71   ? 108 THR B N   1 
ATOM   3133 C  CA  . THR B 1 108 ? -17.978 10.640  40.169  1.00 6.17   ? 108 THR B CA  1 
ATOM   3134 C  C   . THR B 1 108 ? -18.922 10.622  41.374  1.00 5.95   ? 108 THR B C   1 
ATOM   3135 O  O   . THR B 1 108 ? -18.935 11.590  42.126  1.00 6.68   ? 108 THR B O   1 
ATOM   3136 C  CB  . THR B 1 108 ? -16.736 9.750   40.367  1.00 6.91   ? 108 THR B CB  1 
ATOM   3137 O  OG1 . THR B 1 108 ? -15.921 10.244  41.463  1.00 7.31   ? 108 THR B OG1 1 
ATOM   3138 C  CG2 . THR B 1 108 ? -15.881 9.686   39.118  1.00 6.68   ? 108 THR B CG2 1 
ATOM   3139 N  N   . VAL B 1 109 ? -19.685 9.534   41.494  1.00 7.14   ? 109 VAL B N   1 
ATOM   3140 C  CA  . VAL B 1 109 ? -20.651 9.479   42.584  1.00 7.51   ? 109 VAL B CA  1 
ATOM   3141 C  C   . VAL B 1 109 ? -20.330 8.167   43.326  1.00 7.34   ? 109 VAL B C   1 
ATOM   3142 O  O   . VAL B 1 109 ? -20.500 7.058   42.764  1.00 8.34   ? 109 VAL B O   1 
ATOM   3143 C  CB  . VAL B 1 109 ? -22.094 9.445   42.053  1.00 9.58   ? 109 VAL B CB  1 
ATOM   3144 C  CG1 . VAL B 1 109 ? -23.143 9.265   43.189  1.00 10.82  ? 109 VAL B CG1 1 
ATOM   3145 C  CG2 . VAL B 1 109 ? -22.317 10.736  41.248  1.00 10.35  ? 109 VAL B CG2 1 
ATOM   3146 N  N   A ASP B 1 110 ? -19.930 8.235   44.592  0.50 8.02   ? 110 ASP B N   1 
ATOM   3147 N  N   B ASP B 1 110 ? -19.774 8.351   44.537  0.50 8.48   ? 110 ASP B N   1 
ATOM   3148 C  CA  A ASP B 1 110 ? -19.459 7.018   45.263  0.50 8.90   ? 110 ASP B CA  1 
ATOM   3149 C  CA  B ASP B 1 110 ? -19.326 7.174   45.276  0.50 11.58  ? 110 ASP B CA  1 
ATOM   3150 C  C   A ASP B 1 110 ? -18.407 6.242   44.436  0.50 10.09  ? 110 ASP B C   1 
ATOM   3151 C  C   B ASP B 1 110 ? -18.496 6.292   44.344  0.50 12.32  ? 110 ASP B C   1 
ATOM   3152 O  O   A ASP B 1 110 ? -18.336 5.011   44.495  0.50 8.47   ? 110 ASP B O   1 
ATOM   3153 O  O   B ASP B 1 110 ? -18.708 5.088   44.198  0.50 12.90  ? 110 ASP B O   1 
ATOM   3154 C  CB  A ASP B 1 110 ? -20.611 6.141   45.716  0.50 10.54  ? 110 ASP B CB  1 
ATOM   3155 C  CB  B ASP B 1 110 ? -20.474 6.395   45.882  0.50 13.76  ? 110 ASP B CB  1 
ATOM   3156 C  CG  A ASP B 1 110 ? -21.498 6.825   46.726  0.50 8.15   ? 110 ASP B CG  1 
ATOM   3157 C  CG  B ASP B 1 110 ? -21.209 7.222   46.894  0.50 15.15  ? 110 ASP B CG  1 
ATOM   3158 O  OD1 A ASP B 1 110 ? -21.092 7.760   47.366  0.50 9.39   ? 110 ASP B OD1 1 
ATOM   3159 O  OD1 B ASP B 1 110 ? -20.526 8.053   47.566  0.50 16.12  ? 110 ASP B OD1 1 
ATOM   3160 O  OD2 A ASP B 1 110 ? -22.620 6.394   46.835  0.50 10.18  ? 110 ASP B OD2 1 
ATOM   3161 O  OD2 B ASP B 1 110 ? -22.464 7.045   46.957  0.50 15.33  ? 110 ASP B OD2 1 
ATOM   3162 N  N   . LYS B 1 111 ? -17.591 6.984   43.673  1.00 8.98   ? 111 LYS B N   1 
ATOM   3163 C  CA  . LYS B 1 111 ? -16.504 6.458   42.841  1.00 9.83   ? 111 LYS B CA  1 
ATOM   3164 C  C   . LYS B 1 111 ? -17.036 5.938   41.512  1.00 9.22   ? 111 LYS B C   1 
ATOM   3165 O  O   . LYS B 1 111 ? -16.197 5.597   40.670  1.00 10.18  ? 111 LYS B O   1 
ATOM   3166 C  CB  . LYS B 1 111 ? -15.589 5.445   43.543  1.00 11.62  ? 111 LYS B CB  1 
ATOM   3167 C  CG  . LYS B 1 111 ? -14.861 6.014   44.771  1.00 14.74  ? 111 LYS B CG  1 
ATOM   3168 C  CD  . LYS B 1 111 ? -13.901 7.203   44.470  1.00 19.47  ? 111 LYS B CD  1 
ATOM   3169 C  CE  . LYS B 1 111 ? -13.233 7.876   45.671  1.00 21.69  ? 111 LYS B CE  1 
ATOM   3170 N  NZ  . LYS B 1 111 ? -11.971 7.210   45.970  1.00 25.94  ? 111 LYS B NZ  1 
ATOM   3171 N  N   . LYS B 1 112 ? -18.362 5.933   41.273  1.00 8.46   ? 112 LYS B N   1 
ATOM   3172 C  CA  . LYS B 1 112 ? -18.922 5.535   39.992  1.00 9.48   ? 112 LYS B CA  1 
ATOM   3173 C  C   . LYS B 1 112 ? -18.622 6.591   38.926  1.00 7.79   ? 112 LYS B C   1 
ATOM   3174 O  O   . LYS B 1 112 ? -18.878 7.756   39.163  1.00 7.37   ? 112 LYS B O   1 
ATOM   3175 C  CB  . LYS B 1 112 ? -20.439 5.308   40.092  1.00 10.34  ? 112 LYS B CB  1 
ATOM   3176 C  CG  . LYS B 1 112 ? -21.063 4.957   38.754  1.00 12.49  ? 112 LYS B CG  1 
ATOM   3177 C  CD  . LYS B 1 112 ? -22.612 4.872   38.905  1.00 14.16  ? 112 LYS B CD  1 
ATOM   3178 C  CE  . LYS B 1 112 ? -23.246 4.675   37.544  1.00 15.46  ? 112 LYS B CE  1 
ATOM   3179 N  NZ  . LYS B 1 112 ? -22.933 3.356   36.969  1.00 20.06  ? 112 LYS B NZ  1 
ATOM   3180 N  N   A LYS B 1 113 ? -18.114 6.124   37.784  0.50 7.76   ? 113 LYS B N   1 
ATOM   3181 N  N   B LYS B 1 113 ? -18.018 6.164   37.807  0.50 8.08   ? 113 LYS B N   1 
ATOM   3182 C  CA  A LYS B 1 113 ? -17.897 6.956   36.624  0.50 7.70   ? 113 LYS B CA  1 
ATOM   3183 C  CA  B LYS B 1 113 ? -17.812 6.987   36.627  0.50 7.69   ? 113 LYS B CA  1 
ATOM   3184 C  C   A LYS B 1 113 ? -19.051 6.684   35.685  0.50 7.98   ? 113 LYS B C   1 
ATOM   3185 C  C   B LYS B 1 113 ? -18.963 6.702   35.675  0.50 8.06   ? 113 LYS B C   1 
ATOM   3186 O  O   A LYS B 1 113 ? -19.450 5.532   35.475  0.50 11.09  ? 113 LYS B O   1 
ATOM   3187 O  O   B LYS B 1 113 ? -19.290 5.534   35.448  0.50 10.30  ? 113 LYS B O   1 
ATOM   3188 C  CB  A LYS B 1 113 ? -16.612 6.581   35.890  0.50 8.33   ? 113 LYS B CB  1 
ATOM   3189 C  CB  B LYS B 1 113 ? -16.516 6.602   35.909  0.50 8.50   ? 113 LYS B CB  1 
ATOM   3190 C  CG  A LYS B 1 113 ? -15.392 6.913   36.734  0.50 9.55   ? 113 LYS B CG  1 
ATOM   3191 C  CG  B LYS B 1 113 ? -15.260 6.877   36.727  0.50 10.15  ? 113 LYS B CG  1 
ATOM   3192 C  CD  A LYS B 1 113 ? -14.106 6.274   36.208  0.50 11.08  ? 113 LYS B CD  1 
ATOM   3193 C  CD  B LYS B 1 113 ? -14.023 6.362   35.987  0.50 11.53  ? 113 LYS B CD  1 
ATOM   3194 C  CE  A LYS B 1 113 ? -12.890 6.852   36.911  0.50 15.12  ? 113 LYS B CE  1 
ATOM   3195 C  CE  B LYS B 1 113 ? -12.717 6.883   36.560  0.50 14.56  ? 113 LYS B CE  1 
ATOM   3196 N  NZ  A LYS B 1 113 ? -11.636 6.125   36.615  0.50 16.14  ? 113 LYS B NZ  1 
ATOM   3197 N  NZ  B LYS B 1 113 ? -12.394 6.127   37.783  0.50 15.75  ? 113 LYS B NZ  1 
ATOM   3198 N  N   . TYR B 1 114 ? -19.540 7.766   35.100  1.00 7.19   ? 114 TYR B N   1 
ATOM   3199 C  CA  . TYR B 1 114 ? -20.541 7.676   34.059  1.00 7.09   ? 114 TYR B CA  1 
ATOM   3200 C  C   . TYR B 1 114 ? -19.877 7.724   32.687  1.00 7.09   ? 114 TYR B C   1 
ATOM   3201 O  O   . TYR B 1 114 ? -18.681 8.107   32.589  1.00 7.62   ? 114 TYR B O   1 
ATOM   3202 C  CB  . TYR B 1 114 ? -21.585 8.799   34.224  1.00 7.66   ? 114 TYR B CB  1 
ATOM   3203 C  CG  . TYR B 1 114 ? -22.536 8.544   35.348  1.00 7.27   ? 114 TYR B CG  1 
ATOM   3204 C  CD1 . TYR B 1 114 ? -23.762 7.904   35.125  1.00 9.36   ? 114 TYR B CD1 1 
ATOM   3205 C  CD2 . TYR B 1 114 ? -22.298 8.997   36.655  1.00 7.89   ? 114 TYR B CD2 1 
ATOM   3206 C  CE1 . TYR B 1 114 ? -24.676 7.748   36.180  1.00 12.61  ? 114 TYR B CE1 1 
ATOM   3207 C  CE2 . TYR B 1 114 ? -23.164 8.809   37.706  1.00 11.61  ? 114 TYR B CE2 1 
ATOM   3208 C  CZ  . TYR B 1 114 ? -24.368 8.176   37.452  1.00 12.94  ? 114 TYR B CZ  1 
ATOM   3209 O  OH  . TYR B 1 114 ? -25.322 7.970   38.431  1.00 18.22  ? 114 TYR B OH  1 
ATOM   3210 N  N   . ALA B 1 115 ? -20.624 7.397   31.620  1.00 6.80   ? 115 ALA B N   1 
ATOM   3211 C  CA  . ALA B 1 115 ? -20.075 7.410   30.296  1.00 7.14   ? 115 ALA B CA  1 
ATOM   3212 C  C   . ALA B 1 115 ? -19.728 8.798   29.825  1.00 7.24   ? 115 ALA B C   1 
ATOM   3213 O  O   . ALA B 1 115 ? -18.862 8.915   28.943  1.00 7.85   ? 115 ALA B O   1 
ATOM   3214 C  CB  . ALA B 1 115 ? -21.102 6.736   29.398  1.00 8.11   ? 115 ALA B CB  1 
ATOM   3215 N  N   . ALA B 1 116 ? -20.416 9.792   30.309  1.00 7.25   ? 116 ALA B N   1 
ATOM   3216 C  CA  . ALA B 1 116 ? -20.115 11.140  29.864  1.00 6.89   ? 116 ALA B CA  1 
ATOM   3217 C  C   . ALA B 1 116 ? -20.716 12.115  30.855  1.00 6.29   ? 116 ALA B C   1 
ATOM   3218 O  O   . ALA B 1 116 ? -21.435 11.735  31.787  1.00 6.64   ? 116 ALA B O   1 
ATOM   3219 C  CB  . ALA B 1 116 ? -20.660 11.378  28.457  1.00 6.36   ? 116 ALA B CB  1 
ATOM   3220 N  N   . GLU B 1 117 ? -20.323 13.389  30.703  1.00 6.44   ? 117 GLU B N   1 
ATOM   3221 C  CA  . GLU B 1 117 ? -20.865 14.469  31.519  1.00 6.64   ? 117 GLU B CA  1 
ATOM   3222 C  C   . GLU B 1 117 ? -21.074 15.705  30.690  1.00 6.09   ? 117 GLU B C   1 
ATOM   3223 O  O   . GLU B 1 117 ? -20.142 16.046  29.947  1.00 7.33   ? 117 GLU B O   1 
ATOM   3224 C  CB  . GLU B 1 117 ? -19.915 14.671  32.709  1.00 6.46   ? 117 GLU B CB  1 
ATOM   3225 C  CG  . GLU B 1 117 ? -20.449 15.660  33.761  1.00 6.32   ? 117 GLU B CG  1 
ATOM   3226 C  CD  . GLU B 1 117 ? -19.542 15.712  34.980  1.00 6.34   ? 117 GLU B CD  1 
ATOM   3227 O  OE1 . GLU B 1 117 ? -18.864 14.703  35.300  1.00 6.69   ? 117 GLU B OE1 1 
ATOM   3228 O  OE2 . GLU B 1 117 ? -19.531 16.786  35.649  1.00 6.40   ? 117 GLU B OE2 1 
ATOM   3229 N  N   . LEU B 1 118 ? -22.254 16.290  30.793  1.00 6.04   ? 118 LEU B N   1 
ATOM   3230 C  CA  . LEU B 1 118 ? -22.636 17.513  30.117  1.00 6.58   ? 118 LEU B CA  1 
ATOM   3231 C  C   . LEU B 1 118 ? -22.412 18.655  31.093  1.00 6.14   ? 118 LEU B C   1 
ATOM   3232 O  O   . LEU B 1 118 ? -22.818 18.622  32.231  1.00 6.93   ? 118 LEU B O   1 
ATOM   3233 C  CB  . LEU B 1 118 ? -24.143 17.384  29.773  1.00 7.40   ? 118 LEU B CB  1 
ATOM   3234 C  CG  . LEU B 1 118 ? -24.856 18.673  29.402  1.00 7.26   ? 118 LEU B CG  1 
ATOM   3235 C  CD1 . LEU B 1 118 ? -24.280 19.364  28.191  1.00 9.12   ? 118 LEU B CD1 1 
ATOM   3236 C  CD2 . LEU B 1 118 ? -26.403 18.337  29.191  1.00 9.48   ? 118 LEU B CD2 1 
ATOM   3237 N  N   . HIS B 1 119 ? -21.794 19.735  30.583  1.00 6.41   ? 119 HIS B N   1 
ATOM   3238 C  CA  . HIS B 1 119 ? -21.564 20.982  31.371  1.00 6.35   ? 119 HIS B CA  1 
ATOM   3239 C  C   . HIS B 1 119 ? -22.201 22.147  30.672  1.00 6.55   ? 119 HIS B C   1 
ATOM   3240 O  O   . HIS B 1 119 ? -21.864 22.492  29.539  1.00 6.55   ? 119 HIS B O   1 
ATOM   3241 C  CB  . HIS B 1 119 ? -20.051 21.264  31.527  1.00 6.52   ? 119 HIS B CB  1 
ATOM   3242 C  CG  . HIS B 1 119 ? -19.364 20.276  32.414  1.00 5.78   ? 119 HIS B CG  1 
ATOM   3243 N  ND1 . HIS B 1 119 ? -17.968 20.080  32.406  1.00 6.99   ? 119 HIS B ND1 1 
ATOM   3244 C  CD2 . HIS B 1 119 ? -19.886 19.444  33.347  1.00 6.15   ? 119 HIS B CD2 1 
ATOM   3245 C  CE1 . HIS B 1 119 ? -17.693 19.180  33.352  1.00 6.00   ? 119 HIS B CE1 1 
ATOM   3246 N  NE2 . HIS B 1 119 ? -18.860 18.766  33.948  1.00 5.65   ? 119 HIS B NE2 1 
ATOM   3247 N  N   . LEU B 1 120 ? -23.157 22.752  31.376  1.00 6.88   ? 120 LEU B N   1 
ATOM   3248 C  CA  . LEU B 1 120 ? -23.785 24.000  30.899  1.00 8.29   ? 120 LEU B CA  1 
ATOM   3249 C  C   . LEU B 1 120 ? -23.116 25.135  31.702  1.00 6.57   ? 120 LEU B C   1 
ATOM   3250 O  O   . LEU B 1 120 ? -23.273 25.176  32.914  1.00 6.69   ? 120 LEU B O   1 
ATOM   3251 C  CB  . LEU B 1 120 ? -25.276 23.933  31.104  1.00 9.79   ? 120 LEU B CB  1 
ATOM   3252 C  CG  . LEU B 1 120 ? -25.998 22.890  30.197  1.00 11.96  ? 120 LEU B CG  1 
ATOM   3253 C  CD1 . LEU B 1 120 ? -26.747 21.910  31.083  1.00 13.18  ? 120 LEU B CD1 1 
ATOM   3254 C  CD2 . LEU B 1 120 ? -26.858 23.584  29.140  1.00 12.49  ? 120 LEU B CD2 1 
ATOM   3255 N  N   . VAL B 1 121 ? -22.406 26.005  30.990  1.00 7.47   ? 121 VAL B N   1 
ATOM   3256 C  CA  . VAL B 1 121 ? -21.530 27.010  31.648  1.00 7.27   ? 121 VAL B CA  1 
ATOM   3257 C  C   . VAL B 1 121 ? -22.235 28.364  31.595  1.00 7.87   ? 121 VAL B C   1 
ATOM   3258 O  O   . VAL B 1 121 ? -22.654 28.821  30.526  1.00 9.35   ? 121 VAL B O   1 
ATOM   3259 C  CB  . VAL B 1 121 ? -20.203 27.085  30.919  1.00 8.59   ? 121 VAL B CB  1 
ATOM   3260 C  CG1 . VAL B 1 121 ? -19.295 28.146  31.586  1.00 9.40   ? 121 VAL B CG1 1 
ATOM   3261 C  CG2 . VAL B 1 121 ? -19.479 25.745  30.806  1.00 8.11   ? 121 VAL B CG2 1 
ATOM   3262 N  N   . HIS B 1 122 ? -22.358 28.974  32.786  1.00 7.53   ? 122 HIS B N   1 
ATOM   3263 C  CA  . HIS B 1 122 ? -23.055 30.237  32.956  1.00 7.26   ? 122 HIS B CA  1 
ATOM   3264 C  C   . HIS B 1 122 ? -22.114 31.223  33.689  1.00 7.17   ? 122 HIS B C   1 
ATOM   3265 O  O   . HIS B 1 122 ? -21.351 30.810  34.548  1.00 7.82   ? 122 HIS B O   1 
ATOM   3266 C  CB  . HIS B 1 122 ? -24.316 30.095  33.788  1.00 7.54   ? 122 HIS B CB  1 
ATOM   3267 C  CG  . HIS B 1 122 ? -25.196 28.943  33.372  1.00 8.58   ? 122 HIS B CG  1 
ATOM   3268 N  ND1 . HIS B 1 122 ? -24.862 27.652  33.620  1.00 8.25   ? 122 HIS B ND1 1 
ATOM   3269 C  CD2 . HIS B 1 122 ? -26.476 28.904  32.840  1.00 9.78   ? 122 HIS B CD2 1 
ATOM   3270 C  CE1 . HIS B 1 122 ? -25.868 26.881  33.228  1.00 8.25   ? 122 HIS B CE1 1 
ATOM   3271 N  NE2 . HIS B 1 122 ? -26.902 27.584  32.702  1.00 8.95   ? 122 HIS B NE2 1 
ATOM   3272 N  N   . TRP B 1 123 ? -22.313 32.534  33.429  1.00 7.61   ? 123 TRP B N   1 
ATOM   3273 C  CA  . TRP B 1 123 ? -21.447 33.523  34.129  1.00 7.91   ? 123 TRP B CA  1 
ATOM   3274 C  C   . TRP B 1 123 ? -22.362 34.553  34.799  1.00 7.74   ? 123 TRP B C   1 
ATOM   3275 O  O   . TRP B 1 123 ? -23.478 34.875  34.363  1.00 8.77   ? 123 TRP B O   1 
ATOM   3276 C  CB  . TRP B 1 123 ? -20.444 34.188  33.197  1.00 9.20   ? 123 TRP B CB  1 
ATOM   3277 C  CG  . TRP B 1 123 ? -21.036 34.865  32.000  1.00 11.87  ? 123 TRP B CG  1 
ATOM   3278 C  CD1 . TRP B 1 123 ? -21.249 34.273  30.788  1.00 16.42  ? 123 TRP B CD1 1 
ATOM   3279 C  CD2 . TRP B 1 123 ? -21.428 36.210  31.844  1.00 11.85  ? 123 TRP B CD2 1 
ATOM   3280 N  NE1 . TRP B 1 123 ? -21.753 35.181  29.911  1.00 16.97  ? 123 TRP B NE1 1 
ATOM   3281 C  CE2 . TRP B 1 123 ? -21.830 36.392  30.520  1.00 13.62  ? 123 TRP B CE2 1 
ATOM   3282 C  CE3 . TRP B 1 123 ? -21.377 37.325  32.670  1.00 12.05  ? 123 TRP B CE3 1 
ATOM   3283 C  CZ2 . TRP B 1 123 ? -22.277 37.602  30.019  1.00 15.90  ? 123 TRP B CZ2 1 
ATOM   3284 C  CZ3 . TRP B 1 123 ? -21.827 38.530  32.159  1.00 12.97  ? 123 TRP B CZ3 1 
ATOM   3285 C  CH2 . TRP B 1 123 ? -22.278 38.668  30.856  1.00 15.80  ? 123 TRP B CH2 1 
ATOM   3286 N  N   . ASN B 1 124 ? -21.865 35.042  35.943  1.00 8.11   ? 124 ASN B N   1 
ATOM   3287 C  CA  . ASN B 1 124 ? -22.582 35.934  36.829  1.00 8.63   ? 124 ASN B CA  1 
ATOM   3288 C  C   . ASN B 1 124 ? -22.660 37.330  36.208  1.00 8.29   ? 124 ASN B C   1 
ATOM   3289 O  O   . ASN B 1 124 ? -21.647 37.998  36.019  1.00 8.74   ? 124 ASN B O   1 
ATOM   3290 C  CB  . ASN B 1 124 ? -21.793 35.974  38.146  1.00 8.55   ? 124 ASN B CB  1 
ATOM   3291 C  CG  . ASN B 1 124 ? -22.576 36.618  39.257  1.00 8.70   ? 124 ASN B CG  1 
ATOM   3292 O  OD1 . ASN B 1 124 ? -23.432 37.474  39.027  1.00 10.89  ? 124 ASN B OD1 1 
ATOM   3293 N  ND2 . ASN B 1 124 ? -22.285 36.183  40.480  1.00 9.71   ? 124 ASN B ND2 1 
ATOM   3294 N  N   . THR B 1 125 ? -23.895 37.762  35.944  1.00 8.78   ? 125 THR B N   1 
ATOM   3295 C  CA  . THR B 1 125 ? -24.040 39.051  35.238  1.00 11.43  ? 125 THR B CA  1 
ATOM   3296 C  C   . THR B 1 125 ? -23.557 40.261  36.033  1.00 10.76  ? 125 THR B C   1 
ATOM   3297 O  O   . THR B 1 125 ? -23.338 41.313  35.442  1.00 13.70  ? 125 THR B O   1 
ATOM   3298 C  CB  . THR B 1 125 ? -25.478 39.238  34.776  1.00 14.35  ? 125 THR B CB  1 
ATOM   3299 O  OG1 . THR B 1 125 ? -26.288 39.319  35.942  1.00 18.29  ? 125 THR B OG1 1 
ATOM   3300 C  CG2 . THR B 1 125 ? -25.982 38.147  33.834  1.00 16.81  ? 125 THR B CG2 1 
ATOM   3301 N  N   . LYS B 1 126 ? -23.346 40.076  37.369  1.00 10.61  ? 126 LYS B N   1 
ATOM   3302 C  CA  . LYS B 1 126 ? -22.817 41.224  38.103  1.00 13.25  ? 126 LYS B CA  1 
ATOM   3303 C  C   . LYS B 1 126 ? -21.425 41.599  37.645  1.00 12.22  ? 126 LYS B C   1 
ATOM   3304 O  O   . LYS B 1 126 ? -20.923 42.734  37.925  1.00 15.50  ? 126 LYS B O   1 
ATOM   3305 C  CB  . LYS B 1 126 ? -22.969 41.046  39.607  1.00 16.95  ? 126 LYS B CB  1 
ATOM   3306 C  CG  . LYS B 1 126 ? -22.047 40.079  40.290  1.00 16.88  ? 126 LYS B CG  1 
ATOM   3307 C  CD  . LYS B 1 126 ? -22.471 40.051  41.720  1.00 23.48  ? 126 LYS B CD  1 
ATOM   3308 C  CE  . LYS B 1 126 ? -21.628 39.158  42.605  1.00 36.47  ? 126 LYS B CE  1 
ATOM   3309 N  NZ  . LYS B 1 126 ? -20.665 39.906  43.447  1.00 40.56  ? 126 LYS B NZ  1 
ATOM   3310 N  N   . TYR B 1 127 ? -20.715 40.699  36.943  1.00 9.54   ? 127 TYR B N   1 
ATOM   3311 C  CA  . TYR B 1 127 ? -19.329 40.990  36.532  1.00 10.20  ? 127 TYR B CA  1 
ATOM   3312 C  C   . TYR B 1 127 ? -19.266 41.399  35.052  1.00 10.04  ? 127 TYR B C   1 
ATOM   3313 O  O   . TYR B 1 127 ? -18.197 41.692  34.548  1.00 11.20  ? 127 TYR B O   1 
ATOM   3314 C  CB  . TYR B 1 127 ? -18.406 39.808  36.791  1.00 10.84  ? 127 TYR B CB  1 
ATOM   3315 C  CG  . TYR B 1 127 ? -18.348 39.467  38.256  1.00 10.28  ? 127 TYR B CG  1 
ATOM   3316 C  CD1 . TYR B 1 127 ? -17.929 40.427  39.173  1.00 11.32  ? 127 TYR B CD1 1 
ATOM   3317 C  CD2 . TYR B 1 127 ? -18.694 38.199  38.730  1.00 9.84   ? 127 TYR B CD2 1 
ATOM   3318 C  CE1 . TYR B 1 127 ? -17.952 40.109  40.514  1.00 11.20  ? 127 TYR B CE1 1 
ATOM   3319 C  CE2 . TYR B 1 127 ? -18.741 37.872  40.072  1.00 10.14  ? 127 TYR B CE2 1 
ATOM   3320 C  CZ  . TYR B 1 127 ? -18.300 38.857  40.969  1.00 12.30  ? 127 TYR B CZ  1 
ATOM   3321 O  OH  . TYR B 1 127 ? -18.263 38.630  42.306  1.00 13.96  ? 127 TYR B OH  1 
ATOM   3322 N  N   . GLY B 1 128 ? -20.405 41.491  34.369  1.00 11.41  ? 128 GLY B N   1 
ATOM   3323 C  CA  . GLY B 1 128 ? -20.422 42.194  33.097  1.00 11.90  ? 128 GLY B CA  1 
ATOM   3324 C  C   . GLY B 1 128 ? -20.011 41.327  31.891  1.00 11.31  ? 128 GLY B C   1 
ATOM   3325 O  O   . GLY B 1 128 ? -20.620 41.427  30.840  1.00 12.89  ? 128 GLY B O   1 
ATOM   3326 N  N   . ASP B 1 129 ? -18.913 40.578  31.988  1.00 11.09  ? 129 ASP B N   1 
ATOM   3327 C  CA  . ASP B 1 129 ? -18.456 39.748  30.884  1.00 12.44  ? 129 ASP B CA  1 
ATOM   3328 C  C   . ASP B 1 129 ? -17.743 38.529  31.452  1.00 9.84   ? 129 ASP B C   1 
ATOM   3329 O  O   . ASP B 1 129 ? -17.351 38.497  32.641  1.00 10.35  ? 129 ASP B O   1 
ATOM   3330 C  CB  . ASP B 1 129 ? -17.553 40.523  29.894  1.00 11.29  ? 129 ASP B CB  1 
ATOM   3331 C  CG  . ASP B 1 129 ? -16.190 40.965  30.400  1.00 11.88  ? 129 ASP B CG  1 
ATOM   3332 O  OD1 . ASP B 1 129 ? -15.261 40.119  30.648  1.00 15.66  ? 129 ASP B OD1 1 
ATOM   3333 O  OD2 . ASP B 1 129 ? -15.909 42.126  30.392  1.00 17.12  ? 129 ASP B OD2 1 
ATOM   3334 N  N   . VAL B 1 130 ? -17.595 37.496  30.624  1.00 10.94  ? 130 VAL B N   1 
ATOM   3335 C  CA  . VAL B 1 130 ? -17.037 36.249  31.113  1.00 10.85  ? 130 VAL B CA  1 
ATOM   3336 C  C   . VAL B 1 130 ? -15.594 36.376  31.594  1.00 9.60   ? 130 VAL B C   1 
ATOM   3337 O  O   . VAL B 1 130 ? -15.258 35.714  32.538  1.00 9.15   ? 130 VAL B O   1 
ATOM   3338 C  CB  . VAL B 1 130 ? -17.201 35.098  30.131  1.00 11.34  ? 130 VAL B CB  1 
ATOM   3339 C  CG1 . VAL B 1 130 ? -16.433 35.243  28.868  1.00 15.43  ? 130 VAL B CG1 1 
ATOM   3340 C  CG2 . VAL B 1 130 ? -16.962 33.685  30.746  1.00 15.71  ? 130 VAL B CG2 1 
ATOM   3341 N  N   . GLY B 1 131 ? -14.802 37.178  30.848  1.00 11.58  ? 131 GLY B N   1 
ATOM   3342 C  CA  . GLY B 1 131 ? -13.415 37.316  31.235  1.00 12.53  ? 131 GLY B CA  1 
ATOM   3343 C  C   . GLY B 1 131 ? -13.242 37.896  32.646  1.00 9.81   ? 131 GLY B C   1 
ATOM   3344 O  O   . GLY B 1 131 ? -12.377 37.471  33.420  1.00 10.76  ? 131 GLY B O   1 
ATOM   3345 N  N   A LYS B 1 132 ? -14.147 38.822  33.005  0.50 9.84   ? 132 LYS B N   1 
ATOM   3346 N  N   B LYS B 1 132 ? -14.154 38.805  33.008  0.50 9.87   ? 132 LYS B N   1 
ATOM   3347 C  CA  A LYS B 1 132 ? -14.076 39.384  34.356  0.50 10.01  ? 132 LYS B CA  1 
ATOM   3348 C  CA  B LYS B 1 132 ? -14.085 39.372  34.350  0.50 9.94   ? 132 LYS B CA  1 
ATOM   3349 C  C   A LYS B 1 132 ? -14.625 38.347  35.338  0.50 8.37   ? 132 LYS B C   1 
ATOM   3350 C  C   B LYS B 1 132 ? -14.618 38.327  35.334  0.50 8.39   ? 132 LYS B C   1 
ATOM   3351 O  O   A LYS B 1 132 ? -14.086 38.241  36.444  0.50 9.78   ? 132 LYS B O   1 
ATOM   3352 O  O   B LYS B 1 132 ? -14.084 38.216  36.437  0.50 9.69   ? 132 LYS B O   1 
ATOM   3353 C  CB  A LYS B 1 132 ? -14.836 40.709  34.379  0.50 10.53  ? 132 LYS B CB  1 
ATOM   3354 C  CB  B LYS B 1 132 ? -14.917 40.652  34.431  0.50 10.44  ? 132 LYS B CB  1 
ATOM   3355 C  CG  A LYS B 1 132 ? -14.172 41.846  33.654  0.50 14.77  ? 132 LYS B CG  1 
ATOM   3356 C  CG  B LYS B 1 132 ? -14.283 41.937  33.985  0.50 16.28  ? 132 LYS B CG  1 
ATOM   3357 C  CD  A LYS B 1 132 ? -13.027 42.358  34.507  0.50 23.32  ? 132 LYS B CD  1 
ATOM   3358 C  CD  B LYS B 1 132 ? -13.694 41.843  32.635  0.50 21.93  ? 132 LYS B CD  1 
ATOM   3359 C  CE  A LYS B 1 132 ? -12.655 43.775  34.118  0.50 30.66  ? 132 LYS B CE  1 
ATOM   3360 C  CE  B LYS B 1 132 ? -13.779 43.190  31.972  0.50 25.34  ? 132 LYS B CE  1 
ATOM   3361 N  NZ  A LYS B 1 132 ? -11.290 44.119  34.603  0.50 36.82  ? 132 LYS B NZ  1 
ATOM   3362 N  NZ  B LYS B 1 132 ? -13.705 43.033  30.475  0.50 33.24  ? 132 LYS B NZ  1 
ATOM   3363 N  N   . ALA B 1 133 ? -15.667 37.555  34.962  1.00 8.02   ? 133 ALA B N   1 
ATOM   3364 C  CA  . ALA B 1 133 ? -16.238 36.596  35.882  1.00 7.83   ? 133 ALA B CA  1 
ATOM   3365 C  C   . ALA B 1 133 ? -15.203 35.528  36.228  1.00 8.16   ? 133 ALA B C   1 
ATOM   3366 O  O   . ALA B 1 133 ? -15.197 35.028  37.330  1.00 8.30   ? 133 ALA B O   1 
ATOM   3367 C  CB  . ALA B 1 133 ? -17.486 35.935  35.219  1.00 8.04   ? 133 ALA B CB  1 
ATOM   3368 N  N   . LEU B 1 134 ? -14.350 35.163  35.241  1.00 8.38   ? 134 LEU B N   1 
ATOM   3369 C  CA  . LEU B 1 134 ? -13.270 34.187  35.498  1.00 8.54   ? 134 LEU B CA  1 
ATOM   3370 C  C   . LEU B 1 134 ? -12.317 34.533  36.620  1.00 8.98   ? 134 LEU B C   1 
ATOM   3371 O  O   . LEU B 1 134 ? -11.653 33.663  37.157  1.00 9.89   ? 134 LEU B O   1 
ATOM   3372 C  CB  . LEU B 1 134 ? -12.480 33.870  34.217  1.00 9.26   ? 134 LEU B CB  1 
ATOM   3373 C  CG  . LEU B 1 134 ? -13.229 33.144  33.122  1.00 11.59  ? 134 LEU B CG  1 
ATOM   3374 C  CD1 . LEU B 1 134 ? -12.320 33.199  31.879  1.00 17.93  ? 134 LEU B CD1 1 
ATOM   3375 C  CD2 . LEU B 1 134 ? -13.440 31.670  33.451  1.00 13.91  ? 134 LEU B CD2 1 
ATOM   3376 N  N   . GLN B 1 135 ? -12.276 35.819  36.950  1.00 8.91   ? 135 GLN B N   1 
ATOM   3377 C  CA  . GLN B 1 135 ? -11.415 36.303  37.996  1.00 10.36  ? 135 GLN B CA  1 
ATOM   3378 C  C   . GLN B 1 135 ? -12.019 36.371  39.388  1.00 8.95   ? 135 GLN B C   1 
ATOM   3379 O  O   . GLN B 1 135 ? -11.413 36.944  40.299  1.00 11.02  ? 135 GLN B O   1 
ATOM   3380 C  CB  . GLN B 1 135 ? -10.811 37.690  37.609  1.00 15.42  ? 135 GLN B CB  1 
ATOM   3381 C  CG  . GLN B 1 135 ? -10.149 37.603  36.245  1.00 15.65  ? 135 GLN B CG  1 
ATOM   3382 C  CD  . GLN B 1 135 ? -9.648  38.949  35.807  1.00 22.28  ? 135 GLN B CD  1 
ATOM   3383 O  OE1 . GLN B 1 135 ? -8.770  39.547  36.432  1.00 35.08  ? 135 GLN B OE1 1 
ATOM   3384 N  NE2 . GLN B 1 135 ? -10.251 39.447  34.736  1.00 24.53  ? 135 GLN B NE2 1 
ATOM   3385 N  N   . GLN B 1 136 ? -13.240 35.901  39.510  1.00 8.24   ? 136 GLN B N   1 
ATOM   3386 C  CA  . GLN B 1 136 ? -13.987 36.034  40.753  1.00 8.34   ? 136 GLN B CA  1 
ATOM   3387 C  C   . GLN B 1 136 ? -14.393 34.666  41.316  1.00 7.95   ? 136 GLN B C   1 
ATOM   3388 O  O   . GLN B 1 136 ? -14.743 33.740  40.557  1.00 7.78   ? 136 GLN B O   1 
ATOM   3389 C  CB  . GLN B 1 136 ? -15.323 36.722  40.532  1.00 9.52   ? 136 GLN B CB  1 
ATOM   3390 C  CG  . GLN B 1 136 ? -15.140 37.982  39.701  1.00 13.71  ? 136 GLN B CG  1 
ATOM   3391 C  CD  . GLN B 1 136 ? -14.238 39.002  40.221  1.00 14.33  ? 136 GLN B CD  1 
ATOM   3392 O  OE1 . GLN B 1 136 ? -14.066 39.175  41.420  1.00 19.25  ? 136 GLN B OE1 1 
ATOM   3393 N  NE2 . GLN B 1 136 ? -13.526 39.601  39.263  1.00 18.76  ? 136 GLN B NE2 1 
ATOM   3394 N  N   . PRO B 1 137 ? -14.408 34.520  42.672  1.00 8.49   ? 137 PRO B N   1 
ATOM   3395 C  CA  . PRO B 1 137 ? -14.785 33.227  43.259  1.00 7.48   ? 137 PRO B CA  1 
ATOM   3396 C  C   . PRO B 1 137 ? -16.190 32.758  42.979  1.00 8.20   ? 137 PRO B C   1 
ATOM   3397 O  O   . PRO B 1 137 ? -16.422 31.540  43.064  1.00 11.66  ? 137 PRO B O   1 
ATOM   3398 C  CB  . PRO B 1 137 ? -14.528 33.449  44.760  1.00 10.10  ? 137 PRO B CB  1 
ATOM   3399 C  CG  . PRO B 1 137 ? -14.654 34.927  44.913  1.00 14.75  ? 137 PRO B CG  1 
ATOM   3400 C  CD  . PRO B 1 137 ? -14.015 35.532  43.681  1.00 11.00  ? 137 PRO B CD  1 
ATOM   3401 N  N   . ASP B 1 138 ? -17.045 33.717  42.641  1.00 8.30   ? 138 ASP B N   1 
ATOM   3402 C  CA  . ASP B 1 138 ? -18.436 33.398  42.329  1.00 9.09   ? 138 ASP B CA  1 
ATOM   3403 C  C   . ASP B 1 138 ? -18.792 33.816  40.908  1.00 7.31   ? 138 ASP B C   1 
ATOM   3404 O  O   . ASP B 1 138 ? -19.873 34.280  40.623  1.00 9.65   ? 138 ASP B O   1 
ATOM   3405 C  CB  . ASP B 1 138 ? -19.416 33.995  43.343  1.00 9.98   ? 138 ASP B CB  1 
ATOM   3406 C  CG  . ASP B 1 138 ? -19.287 35.517  43.424  1.00 10.27  ? 138 ASP B CG  1 
ATOM   3407 O  OD1 . ASP B 1 138 ? -18.348 36.069  42.840  1.00 10.82  ? 138 ASP B OD1 1 
ATOM   3408 O  OD2 . ASP B 1 138 ? -20.118 36.116  44.154  1.00 14.95  ? 138 ASP B OD2 1 
ATOM   3409 N  N   . GLY B 1 139 ? -17.798 33.741  40.033  1.00 7.61   ? 139 GLY B N   1 
ATOM   3410 C  CA  . GLY B 1 139 ? -17.985 34.222  38.695  1.00 7.59   ? 139 GLY B CA  1 
ATOM   3411 C  C   . GLY B 1 139 ? -18.846 33.308  37.781  1.00 6.18   ? 139 GLY B C   1 
ATOM   3412 O  O   . GLY B 1 139 ? -19.479 33.846  36.874  1.00 7.39   ? 139 GLY B O   1 
ATOM   3413 N  N   . LEU B 1 140 ? -18.657 31.993  37.897  1.00 7.01   ? 140 LEU B N   1 
ATOM   3414 C  CA  . LEU B 1 140 ? -19.326 31.072  36.997  1.00 6.95   ? 140 LEU B CA  1 
ATOM   3415 C  C   . LEU B 1 140 ? -20.177 30.084  37.788  1.00 7.02   ? 140 LEU B C   1 
ATOM   3416 O  O   . LEU B 1 140 ? -19.910 29.807  38.970  1.00 6.77   ? 140 LEU B O   1 
ATOM   3417 C  CB  . LEU B 1 140 ? -18.264 30.283  36.191  1.00 7.33   ? 140 LEU B CB  1 
ATOM   3418 C  CG  . LEU B 1 140 ? -17.680 30.934  34.929  1.00 9.80   ? 140 LEU B CG  1 
ATOM   3419 C  CD1 . LEU B 1 140 ? -17.083 32.334  35.017  1.00 15.30  ? 140 LEU B CD1 1 
ATOM   3420 C  CD2 . LEU B 1 140 ? -16.801 29.953  34.165  1.00 10.94  ? 140 LEU B CD2 1 
ATOM   3421 N  N   . ALA B 1 141 ? -21.204 29.564  37.113  1.00 7.75   ? 141 ALA B N   1 
ATOM   3422 C  CA  . ALA B 1 141 ? -21.976 28.443  37.675  1.00 8.07   ? 141 ALA B CA  1 
ATOM   3423 C  C   . ALA B 1 141 ? -22.040 27.394  36.559  1.00 6.61   ? 141 ALA B C   1 
ATOM   3424 O  O   . ALA B 1 141 ? -22.420 27.767  35.445  1.00 7.74   ? 141 ALA B O   1 
ATOM   3425 C  CB  . ALA B 1 141 ? -23.408 28.876  38.085  1.00 9.19   ? 141 ALA B CB  1 
ATOM   3426 N  N   . VAL B 1 142 ? -21.616 26.189  36.863  1.00 6.57   ? 142 VAL B N   1 
ATOM   3427 C  CA  . VAL B 1 142 ? -21.632 25.138  35.848  1.00 7.79   ? 142 VAL B CA  1 
ATOM   3428 C  C   . VAL B 1 142 ? -22.625 24.117  36.362  1.00 8.01   ? 142 VAL B C   1 
ATOM   3429 O  O   . VAL B 1 142 ? -22.535 23.622  37.449  1.00 7.47   ? 142 VAL B O   1 
ATOM   3430 C  CB  . VAL B 1 142 ? -20.241 24.552  35.517  1.00 7.43   ? 142 VAL B CB  1 
ATOM   3431 C  CG1 . VAL B 1 142 ? -20.436 23.548  34.374  1.00 7.30   ? 142 VAL B CG1 1 
ATOM   3432 C  CG2 . VAL B 1 142 ? -19.277 25.638  35.061  1.00 9.30   ? 142 VAL B CG2 1 
ATOM   3433 N  N   . LEU B 1 143 ? -23.639 23.809  35.490  1.00 8.66   ? 143 LEU B N   1 
ATOM   3434 C  CA  . LEU B 1 143 ? -24.619 22.750  35.739  1.00 10.07  ? 143 LEU B CA  1 
ATOM   3435 C  C   . LEU B 1 143 ? -24.083 21.528  35.056  1.00 8.83   ? 143 LEU B C   1 
ATOM   3436 O  O   . LEU B 1 143 ? -23.903 21.493  33.846  1.00 7.62   ? 143 LEU B O   1 
ATOM   3437 C  CB  . LEU B 1 143 ? -25.929 23.224  35.111  1.00 12.40  ? 143 LEU B CB  1 
ATOM   3438 C  CG  . LEU B 1 143 ? -27.092 22.272  35.270  1.00 19.36  ? 143 LEU B CG  1 
ATOM   3439 C  CD1 . LEU B 1 143 ? -27.351 22.061  36.735  1.00 17.73  ? 143 LEU B CD1 1 
ATOM   3440 C  CD2 . LEU B 1 143 ? -28.341 22.925  34.602  1.00 30.31  ? 143 LEU B CD2 1 
ATOM   3441 N  N   . GLY B 1 144 ? -23.837 20.503  35.871  1.00 7.97   ? 144 GLY B N   1 
ATOM   3442 C  CA  . GLY B 1 144 ? -23.278 19.242  35.371  1.00 6.86   ? 144 GLY B CA  1 
ATOM   3443 C  C   . GLY B 1 144 ? -24.381 18.176  35.381  1.00 5.99   ? 144 GLY B C   1 
ATOM   3444 O  O   . GLY B 1 144 ? -25.091 18.017  36.368  1.00 6.80   ? 144 GLY B O   1 
ATOM   3445 N  N   . ILE B 1 145 ? -24.388 17.374  34.312  1.00 6.72   ? 145 ILE B N   1 
ATOM   3446 C  CA  . ILE B 1 145 ? -25.428 16.342  34.142  1.00 7.41   ? 145 ILE B CA  1 
ATOM   3447 C  C   . ILE B 1 145 ? -24.715 15.100  33.643  1.00 6.69   ? 145 ILE B C   1 
ATOM   3448 O  O   . ILE B 1 145 ? -24.002 15.126  32.625  1.00 6.95   ? 145 ILE B O   1 
ATOM   3449 C  CB  . ILE B 1 145 ? -26.494 16.795  33.107  1.00 9.60   ? 145 ILE B CB  1 
ATOM   3450 C  CG1 . ILE B 1 145 ? -27.155 18.067  33.641  1.00 10.84  ? 145 ILE B CG1 1 
ATOM   3451 C  CG2 . ILE B 1 145 ? -27.520 15.686  32.902  1.00 12.86  ? 145 ILE B CG2 1 
ATOM   3452 C  CD1 . ILE B 1 145 ? -28.160 18.693  32.684  1.00 11.92  ? 145 ILE B CD1 1 
ATOM   3453 N  N   . PHE B 1 146 ? -24.886 13.993  34.366  1.00 6.50   ? 146 PHE B N   1 
ATOM   3454 C  CA  . PHE B 1 146 ? -24.272 12.751  33.956  1.00 7.61   ? 146 PHE B CA  1 
ATOM   3455 C  C   . PHE B 1 146 ? -25.033 12.124  32.790  1.00 8.26   ? 146 PHE B C   1 
ATOM   3456 O  O   . PHE B 1 146 ? -26.303 12.222  32.726  1.00 9.38   ? 146 PHE B O   1 
ATOM   3457 C  CB  . PHE B 1 146 ? -24.304 11.750  35.115  1.00 8.05   ? 146 PHE B CB  1 
ATOM   3458 C  CG  . PHE B 1 146 ? -23.469 12.233  36.281  1.00 6.21   ? 146 PHE B CG  1 
ATOM   3459 C  CD1 . PHE B 1 146 ? -22.073 12.396  36.124  1.00 6.30   ? 146 PHE B CD1 1 
ATOM   3460 C  CD2 . PHE B 1 146 ? -24.039 12.517  37.508  1.00 7.41   ? 146 PHE B CD2 1 
ATOM   3461 C  CE1 . PHE B 1 146 ? -21.286 12.801  37.212  1.00 7.02   ? 146 PHE B CE1 1 
ATOM   3462 C  CE2 . PHE B 1 146 ? -23.256 12.917  38.588  1.00 8.33   ? 146 PHE B CE2 1 
ATOM   3463 C  CZ  . PHE B 1 146 ? -21.854 13.017  38.429  1.00 7.54   ? 146 PHE B CZ  1 
ATOM   3464 N  N   . LEU B 1 147 ? -24.342 11.365  31.957  1.00 7.97   ? 147 LEU B N   1 
ATOM   3465 C  CA  . LEU B 1 147 ? -24.950 10.541  30.875  1.00 8.02   ? 147 LEU B CA  1 
ATOM   3466 C  C   . LEU B 1 147 ? -24.562 9.112   31.149  1.00 7.41   ? 147 LEU B C   1 
ATOM   3467 O  O   . LEU B 1 147 ? -23.405 8.742   31.315  1.00 7.62   ? 147 LEU B O   1 
ATOM   3468 C  CB  . LEU B 1 147 ? -24.353 10.952  29.522  1.00 8.43   ? 147 LEU B CB  1 
ATOM   3469 C  CG  . LEU B 1 147 ? -24.894 12.222  28.857  1.00 9.86   ? 147 LEU B CG  1 
ATOM   3470 C  CD1 . LEU B 1 147 ? -24.701 13.521  29.660  1.00 9.34   ? 147 LEU B CD1 1 
ATOM   3471 C  CD2 . LEU B 1 147 ? -24.270 12.371  27.527  1.00 9.95   ? 147 LEU B CD2 1 
ATOM   3472 N  N   . LYS B 1 148 ? -25.609 8.257   31.087  1.00 7.56   ? 148 LYS B N   1 
ATOM   3473 C  CA  . LYS B 1 148 ? -25.442 6.815   31.055  1.00 7.80   ? 148 LYS B CA  1 
ATOM   3474 C  C   . LYS B 1 148 ? -25.917 6.299   29.698  1.00 7.48   ? 148 LYS B C   1 
ATOM   3475 O  O   . LYS B 1 148 ? -26.767 6.916   29.077  1.00 9.46   ? 148 LYS B O   1 
ATOM   3476 C  CB  . LYS B 1 148 ? -26.192 6.095   32.180  1.00 10.04  ? 148 LYS B CB  1 
ATOM   3477 C  CG  . LYS B 1 148 ? -27.659 6.358   32.181  1.00 12.21  ? 148 LYS B CG  1 
ATOM   3478 C  CD  . LYS B 1 148 ? -28.373 5.625   33.368  1.00 14.42  ? 148 LYS B CD  1 
ATOM   3479 C  CE  . LYS B 1 148 ? -29.834 5.432   33.209  1.00 24.77  ? 148 LYS B CE  1 
ATOM   3480 N  NZ  . LYS B 1 148 ? -30.293 4.885   34.517  1.00 34.64  ? 148 LYS B NZ  1 
ATOM   3481 N  N   . VAL B 1 149 ? -25.449 5.131   29.337  1.00 9.23   ? 149 VAL B N   1 
ATOM   3482 C  CA  . VAL B 1 149 ? -25.810 4.515   28.046  1.00 9.70   ? 149 VAL B CA  1 
ATOM   3483 C  C   . VAL B 1 149 ? -26.946 3.544   28.214  1.00 9.81   ? 149 VAL B C   1 
ATOM   3484 O  O   . VAL B 1 149 ? -26.870 2.585   28.980  1.00 11.65  ? 149 VAL B O   1 
ATOM   3485 C  CB  . VAL B 1 149 ? -24.575 3.859   27.409  1.00 10.83  ? 149 VAL B CB  1 
ATOM   3486 C  CG1 . VAL B 1 149 ? -24.968 3.077   26.133  1.00 14.37  ? 149 VAL B CG1 1 
ATOM   3487 C  CG2 . VAL B 1 149 ? -23.431 4.863   27.104  1.00 11.87  ? 149 VAL B CG2 1 
ATOM   3488 N  N   . GLY B 1 150 ? -28.026 3.837   27.477  1.00 9.84   ? 150 GLY B N   1 
ATOM   3489 C  CA  . GLY B 1 150 ? -29.231 3.027   27.518  1.00 12.69  ? 150 GLY B CA  1 
ATOM   3490 C  C   . GLY B 1 150 ? -30.112 3.465   26.361  1.00 11.88  ? 150 GLY B C   1 
ATOM   3491 O  O   . GLY B 1 150 ? -29.770 3.372   25.178  1.00 11.28  ? 150 GLY B O   1 
ATOM   3492 N  N   . SER B 1 151 ? -31.290 3.989   26.717  1.00 11.97  ? 151 SER B N   1 
ATOM   3493 C  CA  . SER B 1 151 ? -32.207 4.592   25.738  1.00 13.77  ? 151 SER B CA  1 
ATOM   3494 C  C   . SER B 1 151 ? -31.649 5.875   25.099  1.00 11.61  ? 151 SER B C   1 
ATOM   3495 O  O   . SER B 1 151 ? -30.873 6.593   25.728  1.00 12.41  ? 151 SER B O   1 
ATOM   3496 C  CB  . SER B 1 151 ? -33.607 4.828   26.309  1.00 20.58  ? 151 SER B CB  1 
ATOM   3497 O  OG  . SER B 1 151 ? -34.125 3.701   26.989  1.00 28.41  ? 151 SER B OG  1 
ATOM   3498 N  N   . ALA B 1 152 ? -32.028 6.245   23.869  1.00 11.71  ? 152 ALA B N   1 
ATOM   3499 C  CA  . ALA B 1 152 ? -31.523 7.483   23.259  1.00 12.83  ? 152 ALA B CA  1 
ATOM   3500 C  C   . ALA B 1 152 ? -32.152 8.668   23.973  1.00 11.71  ? 152 ALA B C   1 
ATOM   3501 O  O   . ALA B 1 152 ? -33.309 8.611   24.370  1.00 13.73  ? 152 ALA B O   1 
ATOM   3502 C  CB  . ALA B 1 152 ? -31.856 7.486   21.773  1.00 16.03  ? 152 ALA B CB  1 
ATOM   3503 N  N   . LYS B 1 153 ? -31.528 9.810   23.868  1.00 11.81  ? 153 LYS B N   1 
ATOM   3504 C  CA  . LYS B 1 153 ? -32.061 11.038  24.363  1.00 12.71  ? 153 LYS B CA  1 
ATOM   3505 C  C   . LYS B 1 153 ? -32.528 11.803  23.125  1.00 13.86  ? 153 LYS B C   1 
ATOM   3506 O  O   . LYS B 1 153 ? -31.669 12.252  22.344  1.00 14.74  ? 153 LYS B O   1 
ATOM   3507 C  CB  . LYS B 1 153 ? -30.962 11.860  25.073  1.00 13.24  ? 153 LYS B CB  1 
ATOM   3508 C  CG  . LYS B 1 153 ? -31.554 13.089  25.738  1.00 16.95  ? 153 LYS B CG  1 
ATOM   3509 C  CD  . LYS B 1 153 ? -32.329 12.744  26.969  1.00 18.64  ? 153 LYS B CD  1 
ATOM   3510 C  CE  . LYS B 1 153 ? -32.407 13.958  27.847  1.00 19.17  ? 153 LYS B CE  1 
ATOM   3511 N  NZ  . LYS B 1 153 ? -33.337 13.589  28.915  1.00 20.12  ? 153 LYS B NZ  1 
ATOM   3512 N  N   . PRO B 1 154 ? -33.860 11.905  22.842  1.00 13.80  ? 154 PRO B N   1 
ATOM   3513 C  CA  . PRO B 1 154 ? -34.233 12.487  21.552  1.00 15.69  ? 154 PRO B CA  1 
ATOM   3514 C  C   . PRO B 1 154 ? -33.710 13.917  21.384  1.00 15.04  ? 154 PRO B C   1 
ATOM   3515 O  O   . PRO B 1 154 ? -33.324 14.302  20.284  1.00 18.34  ? 154 PRO B O   1 
ATOM   3516 C  CB  . PRO B 1 154 ? -35.748 12.469  21.628  1.00 15.90  ? 154 PRO B CB  1 
ATOM   3517 C  CG  . PRO B 1 154 ? -36.106 11.367  22.602  1.00 21.23  ? 154 PRO B CG  1 
ATOM   3518 C  CD  . PRO B 1 154 ? -35.020 11.428  23.631  1.00 15.22  ? 154 PRO B CD  1 
ATOM   3519 N  N   . GLY B 1 155 ? -33.664 14.678  22.493  1.00 14.73  ? 155 GLY B N   1 
ATOM   3520 C  CA  . GLY B 1 155 ? -33.249 16.081  22.493  1.00 18.36  ? 155 GLY B CA  1 
ATOM   3521 C  C   . GLY B 1 155 ? -31.759 16.282  22.162  1.00 16.52  ? 155 GLY B C   1 
ATOM   3522 O  O   . GLY B 1 155 ? -31.296 17.371  21.835  1.00 19.13  ? 155 GLY B O   1 
ATOM   3523 N  N   . LEU B 1 156 ? -30.979 15.210  22.241  1.00 14.61  ? 156 LEU B N   1 
ATOM   3524 C  CA  . LEU B 1 156 ? -29.584 15.191  21.867  1.00 13.50  ? 156 LEU B CA  1 
ATOM   3525 C  C   . LEU B 1 156 ? -29.307 14.974  20.388  1.00 18.27  ? 156 LEU B C   1 
ATOM   3526 O  O   . LEU B 1 156 ? -28.232 15.302  19.889  1.00 16.42  ? 156 LEU B O   1 
ATOM   3527 C  CB  . LEU B 1 156 ? -28.832 14.183  22.730  1.00 15.21  ? 156 LEU B CB  1 
ATOM   3528 C  CG  . LEU B 1 156 ? -27.311 14.084  22.539  1.00 14.28  ? 156 LEU B CG  1 
ATOM   3529 C  CD1 . LEU B 1 156 ? -26.553 15.397  22.874  1.00 15.47  ? 156 LEU B CD1 1 
ATOM   3530 C  CD2 . LEU B 1 156 ? -26.707 12.942  23.353  1.00 12.30  ? 156 LEU B CD2 1 
ATOM   3531 N  N   . GLN B 1 157 ? -30.289 14.424  19.652  1.00 16.24  ? 157 GLN B N   1 
ATOM   3532 C  CA  . GLN B 1 157 ? -29.947 13.917  18.329  1.00 17.44  ? 157 GLN B CA  1 
ATOM   3533 C  C   . GLN B 1 157 ? -29.528 15.057  17.385  1.00 15.09  ? 157 GLN B C   1 
ATOM   3534 O  O   . GLN B 1 157 ? -28.704 14.859  16.519  1.00 16.04  ? 157 GLN B O   1 
ATOM   3535 C  CB  . GLN B 1 157 ? -31.139 13.119  17.751  1.00 18.51  ? 157 GLN B CB  1 
ATOM   3536 C  CG  . GLN B 1 157 ? -30.719 12.413  16.446  1.00 19.72  ? 157 GLN B CG  1 
ATOM   3537 C  CD  . GLN B 1 157 ? -29.636 11.387  16.687  1.00 19.44  ? 157 GLN B CD  1 
ATOM   3538 O  OE1 . GLN B 1 157 ? -29.529 10.843  17.798  1.00 20.00  ? 157 GLN B OE1 1 
ATOM   3539 N  NE2 . GLN B 1 157 ? -28.819 11.104  15.643  1.00 22.23  ? 157 GLN B NE2 1 
ATOM   3540 N  N   . LYS B 1 158 ? -30.125 16.269  17.501  1.00 17.92  ? 158 LYS B N   1 
ATOM   3541 C  CA  . LYS B 1 158 ? -29.710 17.366  16.634  1.00 16.97  ? 158 LYS B CA  1 
ATOM   3542 C  C   . LYS B 1 158 ? -28.217 17.654  16.757  1.00 14.46  ? 158 LYS B C   1 
ATOM   3543 O  O   . LYS B 1 158 ? -27.537 18.059  15.800  1.00 17.95  ? 158 LYS B O   1 
ATOM   3544 C  CB  . LYS B 1 158 ? -30.616 18.599  16.792  1.00 18.15  ? 158 LYS B CB  1 
ATOM   3545 C  CG  . LYS B 1 158 ? -31.942 18.512  16.011  1.00 27.98  ? 158 LYS B CG  1 
ATOM   3546 N  N   . VAL B 1 159 ? -27.691 17.531  17.986  1.00 16.97  ? 159 VAL B N   1 
ATOM   3547 C  CA  . VAL B 1 159 ? -26.284 17.825  18.225  1.00 15.97  ? 159 VAL B CA  1 
ATOM   3548 C  C   . VAL B 1 159 ? -25.479 16.673  17.612  1.00 16.38  ? 159 VAL B C   1 
ATOM   3549 O  O   . VAL B 1 159 ? -24.622 16.932  16.804  1.00 16.31  ? 159 VAL B O   1 
ATOM   3550 C  CB  . VAL B 1 159 ? -26.024 17.836  19.735  1.00 17.07  ? 159 VAL B CB  1 
ATOM   3551 C  CG1 . VAL B 1 159 ? -24.524 17.759  20.009  1.00 18.37  ? 159 VAL B CG1 1 
ATOM   3552 C  CG2 . VAL B 1 159 ? -26.612 19.072  20.390  1.00 19.85  ? 159 VAL B CG2 1 
ATOM   3553 N  N   . VAL B 1 160 ? -25.836 15.410  17.872  1.00 15.11  ? 160 VAL B N   1 
ATOM   3554 C  CA  . VAL B 1 160 ? -25.066 14.308  17.300  1.00 17.62  ? 160 VAL B CA  1 
ATOM   3555 C  C   . VAL B 1 160 ? -25.045 14.381  15.776  1.00 17.04  ? 160 VAL B C   1 
ATOM   3556 O  O   . VAL B 1 160 ? -24.033 14.086  15.174  1.00 17.88  ? 160 VAL B O   1 
ATOM   3557 C  CB  . VAL B 1 160 ? -25.625 12.963  17.814  1.00 23.76  ? 160 VAL B CB  1 
ATOM   3558 C  CG1 . VAL B 1 160 ? -25.402 11.700  16.894  1.00 29.45  ? 160 VAL B CG1 1 
ATOM   3559 C  CG2 . VAL B 1 160 ? -25.210 12.768  19.269  1.00 25.26  ? 160 VAL B CG2 1 
ATOM   3560 N  N   . ASP B 1 161 ? -26.144 14.807  15.140  1.00 17.59  ? 161 ASP B N   1 
ATOM   3561 C  CA  . ASP B 1 161 ? -26.215 14.698  13.684  1.00 18.47  ? 161 ASP B CA  1 
ATOM   3562 C  C   . ASP B 1 161 ? -25.359 15.727  12.965  1.00 21.70  ? 161 ASP B C   1 
ATOM   3563 O  O   . ASP B 1 161 ? -25.126 15.547  11.775  1.00 27.15  ? 161 ASP B O   1 
ATOM   3564 C  CB  . ASP B 1 161 ? -27.666 14.801  13.229  1.00 23.22  ? 161 ASP B CB  1 
ATOM   3565 C  CG  . ASP B 1 161 ? -28.322 13.436  13.260  1.00 23.00  ? 161 ASP B CG  1 
ATOM   3566 O  OD1 . ASP B 1 161 ? -27.549 12.425  13.216  1.00 23.51  ? 161 ASP B OD1 1 
ATOM   3567 O  OD2 . ASP B 1 161 ? -29.575 13.369  13.425  1.00 29.28  ? 161 ASP B OD2 1 
ATOM   3568 N  N   . VAL B 1 162 ? -24.795 16.736  13.671  1.00 19.44  ? 162 VAL B N   1 
ATOM   3569 C  CA  . VAL B 1 162 ? -24.049 17.788  13.032  1.00 21.93  ? 162 VAL B CA  1 
ATOM   3570 C  C   . VAL B 1 162 ? -22.555 17.512  13.274  1.00 20.24  ? 162 VAL B C   1 
ATOM   3571 O  O   . VAL B 1 162 ? -21.730 18.196  12.696  1.00 24.03  ? 162 VAL B O   1 
ATOM   3572 C  CB  . VAL B 1 162 ? -24.543 19.160  13.557  1.00 26.52  ? 162 VAL B CB  1 
ATOM   3573 C  CG1 . VAL B 1 162 ? -23.892 19.513  14.893  1.00 26.32  ? 162 VAL B CG1 1 
ATOM   3574 C  CG2 . VAL B 1 162 ? -24.359 20.304  12.577  1.00 32.50  ? 162 VAL B CG2 1 
ATOM   3575 N  N   . LEU B 1 163 ? -22.176 16.516  14.110  1.00 19.79  ? 163 LEU B N   1 
ATOM   3576 C  CA  . LEU B 1 163 ? -20.767 16.352  14.473  1.00 18.48  ? 163 LEU B CA  1 
ATOM   3577 C  C   . LEU B 1 163 ? -19.870 15.969  13.270  1.00 17.42  ? 163 LEU B C   1 
ATOM   3578 O  O   . LEU B 1 163 ? -18.656 16.295  13.237  1.00 21.84  ? 163 LEU B O   1 
ATOM   3579 C  CB  . LEU B 1 163 ? -20.562 15.366  15.613  1.00 16.30  ? 163 LEU B CB  1 
ATOM   3580 C  CG  . LEU B 1 163 ? -21.251 15.697  16.930  1.00 14.59  ? 163 LEU B CG  1 
ATOM   3581 C  CD1 . LEU B 1 163 ? -20.948 14.556  17.926  1.00 15.23  ? 163 LEU B CD1 1 
ATOM   3582 C  CD2 . LEU B 1 163 ? -20.641 16.991  17.446  1.00 15.60  ? 163 LEU B CD2 1 
ATOM   3583 N  N   . ASP B 1 164 ? -20.434 15.276  12.269  1.00 20.64  ? 164 ASP B N   1 
ATOM   3584 C  CA  . ASP B 1 164 ? -19.600 14.942  11.123  1.00 23.64  ? 164 ASP B CA  1 
ATOM   3585 C  C   . ASP B 1 164 ? -19.173 16.217  10.386  1.00 25.28  ? 164 ASP B C   1 
ATOM   3586 O  O   . ASP B 1 164 ? -18.218 16.161  9.618   1.00 28.45  ? 164 ASP B O   1 
ATOM   3587 C  CB  . ASP B 1 164 ? -20.327 14.074  10.083  1.00 26.91  ? 164 ASP B CB  1 
ATOM   3588 C  CG  . ASP B 1 164 ? -21.307 14.937  9.316   1.00 42.01  ? 164 ASP B CG  1 
ATOM   3589 O  OD1 . ASP B 1 164 ? -22.282 15.378  9.928   1.00 38.14  ? 164 ASP B OD1 1 
ATOM   3590 O  OD2 . ASP B 1 164 ? -21.112 15.155  8.072   1.00 55.74  ? 164 ASP B OD2 1 
ATOM   3591 N  N   . SER B 1 165 ? -19.879 17.344  10.573  1.00 22.48  ? 165 SER B N   1 
ATOM   3592 C  CA  . SER B 1 165 ? -19.464 18.599  9.929   1.00 24.56  ? 165 SER B CA  1 
ATOM   3593 C  C   . SER B 1 165 ? -18.381 19.368  10.691  1.00 24.40  ? 165 SER B C   1 
ATOM   3594 O  O   . SER B 1 165 ? -17.902 20.376  10.194  1.00 27.11  ? 165 SER B O   1 
ATOM   3595 C  CB  . SER B 1 165 ? -20.644 19.489  9.653   1.00 26.38  ? 165 SER B CB  1 
ATOM   3596 O  OG  . SER B 1 165 ? -21.129 20.091  10.862  1.00 27.38  ? 165 SER B OG  1 
ATOM   3597 N  N   . ILE B 1 166 ? -18.031 18.904  11.882  1.00 24.24  ? 166 ILE B N   1 
ATOM   3598 C  CA  . ILE B 1 166 ? -17.024 19.572  12.715  1.00 23.77  ? 166 ILE B CA  1 
ATOM   3599 C  C   . ILE B 1 166 ? -16.014 18.545  13.234  1.00 19.67  ? 166 ILE B C   1 
ATOM   3600 O  O   . ILE B 1 166 ? -15.635 18.537  14.397  1.00 21.67  ? 166 ILE B O   1 
ATOM   3601 C  CB  . ILE B 1 166 ? -17.657 20.441  13.836  1.00 22.11  ? 166 ILE B CB  1 
ATOM   3602 C  CG1 . ILE B 1 166 ? -18.637 19.672  14.744  1.00 19.66  ? 166 ILE B CG1 1 
ATOM   3603 C  CG2 . ILE B 1 166 ? -18.297 21.686  13.255  1.00 23.27  ? 166 ILE B CG2 1 
ATOM   3604 C  CD1 . ILE B 1 166 ? -18.523 20.257  16.194  1.00 18.98  ? 166 ILE B CD1 1 
ATOM   3605 N  N   . LYS B 1 167 ? -15.629 17.582  12.354  1.00 20.75  ? 167 LYS B N   1 
ATOM   3606 C  CA  . LYS B 1 167 ? -14.865 16.429  12.826  1.00 19.88  ? 167 LYS B CA  1 
ATOM   3607 C  C   . LYS B 1 167 ? -13.550 16.834  13.512  1.00 20.80  ? 167 LYS B C   1 
ATOM   3608 O  O   . LYS B 1 167 ? -13.100 16.178  14.456  1.00 19.73  ? 167 LYS B O   1 
ATOM   3609 C  CB  . LYS B 1 167 ? -14.527 15.507  11.654  1.00 18.92  ? 167 LYS B CB  1 
ATOM   3610 C  CG  . LYS B 1 167 ? -13.837 14.230  12.096  1.00 19.53  ? 167 LYS B CG  1 
ATOM   3611 C  CD  . LYS B 1 167 ? -13.669 13.315  10.899  1.00 29.96  ? 167 LYS B CD  1 
ATOM   3612 C  CE  . LYS B 1 167 ? -12.520 12.321  10.965  1.00 33.73  ? 167 LYS B CE  1 
ATOM   3613 N  NZ  . LYS B 1 167 ? -12.583 11.317  9.849   1.00 46.23  ? 167 LYS B NZ  1 
ATOM   3614 N  N   . THR B 1 168 ? -12.919 17.890  12.972  1.00 22.01  ? 168 THR B N   1 
ATOM   3615 C  CA  . THR B 1 168 ? -11.594 18.307  13.383  1.00 20.42  ? 168 THR B CA  1 
ATOM   3616 C  C   . THR B 1 168 ? -11.546 19.706  14.018  1.00 12.30  ? 168 THR B C   1 
ATOM   3617 O  O   . THR B 1 168 ? -12.462 20.507  13.868  1.00 19.85  ? 168 THR B O   1 
ATOM   3618 C  CB  . THR B 1 168 ? -10.644 18.217  12.164  1.00 20.80  ? 168 THR B CB  1 
ATOM   3619 O  OG1 . THR B 1 168 ? -11.250 18.962  11.104  1.00 22.06  ? 168 THR B OG1 1 
ATOM   3620 C  CG2 . THR B 1 168 ? -10.287 16.784  11.779  1.00 21.39  ? 168 THR B CG2 1 
ATOM   3621 N  N   . LYS B 1 169 ? -10.495 19.799  14.826  1.00 17.49  ? 169 LYS B N   1 
ATOM   3622 C  CA  . LYS B 1 169 ? -10.053 20.954  15.598  1.00 21.65  ? 169 LYS B CA  1 
ATOM   3623 C  C   . LYS B 1 169 ? -10.139 22.206  14.760  1.00 21.30  ? 169 LYS B C   1 
ATOM   3624 O  O   . LYS B 1 169 ? -9.514  22.224  13.697  1.00 27.35  ? 169 LYS B O   1 
ATOM   3625 C  CB  . LYS B 1 169 ? -8.621  20.785  16.158  1.00 21.57  ? 169 LYS B CB  1 
ATOM   3626 C  CG  . LYS B 1 169 ? -8.044  21.892  17.044  1.00 21.11  ? 169 LYS B CG  1 
ATOM   3627 C  CD  . LYS B 1 169 ? -6.537  21.584  17.189  1.00 40.39  ? 169 LYS B CD  1 
ATOM   3628 C  CE  . LYS B 1 169 ? -5.955  21.402  18.592  1.00 58.10  ? 169 LYS B CE  1 
ATOM   3629 N  NZ  . LYS B 1 169 ? -6.720  20.477  19.517  1.00 55.59  ? 169 LYS B NZ  1 
ATOM   3630 N  N   . GLY B 1 170 ? -11.028 23.128  15.189  1.00 25.22  ? 170 GLY B N   1 
ATOM   3631 C  CA  . GLY B 1 170 ? -11.171 24.447  14.559  1.00 27.51  ? 170 GLY B CA  1 
ATOM   3632 C  C   . GLY B 1 170 ? -12.385 24.634  13.619  1.00 24.33  ? 170 GLY B C   1 
ATOM   3633 O  O   . GLY B 1 170 ? -12.559 25.705  13.088  1.00 29.25  ? 170 GLY B O   1 
ATOM   3634 N  N   . LYS B 1 171 ? -13.270 23.636  13.400  1.00 20.09  ? 171 LYS B N   1 
ATOM   3635 C  CA  . LYS B 1 171 ? -14.557 23.691  12.639  1.00 24.26  ? 171 LYS B CA  1 
ATOM   3636 C  C   . LYS B 1 171 ? -15.813 24.117  13.467  1.00 20.38  ? 171 LYS B C   1 
ATOM   3637 O  O   . LYS B 1 171 ? -15.913 23.629  14.587  1.00 22.41  ? 171 LYS B O   1 
ATOM   3638 C  CB  . LYS B 1 171 ? -14.756 22.328  11.906  1.00 22.88  ? 171 LYS B CB  1 
ATOM   3639 C  CG  . LYS B 1 171 ? -13.525 21.793  11.148  1.00 30.64  ? 171 LYS B CG  1 
ATOM   3640 C  CD  . LYS B 1 171 ? -13.735 20.647  10.131  1.00 37.74  ? 171 LYS B CD  1 
ATOM   3641 C  CE  . LYS B 1 171 ? -12.932 20.831  8.857   1.00 51.20  ? 171 LYS B CE  1 
ATOM   3642 N  NZ  . LYS B 1 171 ? -13.358 22.023  8.075   1.00 43.61  ? 171 LYS B NZ  1 
ATOM   3643 N  N   A SER B 1 172 ? -16.811 24.823  12.856  0.50 17.34  ? 172 SER B N   1 
ATOM   3644 N  N   B SER B 1 172 ? -16.592 25.104  12.974  0.50 15.43  ? 172 SER B N   1 
ATOM   3645 C  CA  A SER B 1 172 ? -17.973 25.514  13.342  0.50 19.80  ? 172 SER B CA  1 
ATOM   3646 C  CA  B SER B 1 172 ? -17.945 25.355  13.465  0.50 20.89  ? 172 SER B CA  1 
ATOM   3647 C  C   A SER B 1 172 ? -19.118 25.251  12.338  0.50 17.97  ? 172 SER B C   1 
ATOM   3648 C  C   B SER B 1 172 ? -19.051 25.188  12.397  0.50 16.02  ? 172 SER B C   1 
ATOM   3649 O  O   A SER B 1 172 ? -18.920 25.118  11.108  0.50 21.90  ? 172 SER B O   1 
ATOM   3650 O  O   B SER B 1 172 ? -18.691 25.157  11.179  0.50 27.39  ? 172 SER B O   1 
ATOM   3651 C  CB  A SER B 1 172 ? -17.640 27.022  13.492  0.50 17.99  ? 172 SER B CB  1 
ATOM   3652 C  CB  B SER B 1 172 ? -18.027 26.742  14.059  0.50 20.06  ? 172 SER B CB  1 
ATOM   3653 O  OG  A SER B 1 172 ? -16.291 27.373  13.100  0.50 13.90  ? 172 SER B OG  1 
ATOM   3654 O  OG  B SER B 1 172 ? -17.654 27.724  13.083  0.50 18.70  ? 172 SER B OG  1 
ATOM   3655 N  N   . ALA B 1 173 ? -20.332 25.221  12.835  1.00 21.45  ? 173 ALA B N   1 
ATOM   3656 C  CA  . ALA B 1 173 ? -21.580 25.234  12.058  1.00 21.47  ? 173 ALA B CA  1 
ATOM   3657 C  C   . ALA B 1 173 ? -22.658 26.067  12.741  1.00 16.59  ? 173 ALA B C   1 
ATOM   3658 O  O   . ALA B 1 173 ? -22.771 26.116  13.969  1.00 16.80  ? 173 ALA B O   1 
ATOM   3659 C  CB  . ALA B 1 173 ? -21.975 23.787  11.896  1.00 28.33  ? 173 ALA B CB  1 
ATOM   3660 N  N   . ASP B 1 174 ? -23.521 26.686  11.947  1.00 22.91  ? 174 ASP B N   1 
ATOM   3661 C  CA  . ASP B 1 174 ? -24.628 27.377  12.494  1.00 20.27  ? 174 ASP B CA  1 
ATOM   3662 C  C   . ASP B 1 174 ? -25.376 26.290  13.254  1.00 24.76  ? 174 ASP B C   1 
ATOM   3663 O  O   . ASP B 1 174 ? -25.289 25.112  12.869  1.00 31.41  ? 174 ASP B O   1 
ATOM   3664 C  CB  . ASP B 1 174 ? -25.433 28.086  11.385  1.00 36.29  ? 174 ASP B CB  1 
ATOM   3665 C  CG  . ASP B 1 174 ? -24.576 28.919  10.439  1.00 42.38  ? 174 ASP B CG  1 
ATOM   3666 O  OD1 . ASP B 1 174 ? -23.702 29.679  10.930  1.00 43.22  ? 174 ASP B OD1 1 
ATOM   3667 O  OD2 . ASP B 1 174 ? -24.778 28.800  9.210   1.00 51.07  ? 174 ASP B OD2 1 
ATOM   3668 N  N   . PHE B 1 175 ? -25.968 26.679  14.365  1.00 19.38  ? 175 PHE B N   1 
ATOM   3669 C  CA  . PHE B 1 175 ? -26.528 25.743  15.278  1.00 20.51  ? 175 PHE B CA  1 
ATOM   3670 C  C   . PHE B 1 175 ? -27.495 26.603  15.986  1.00 23.83  ? 175 PHE B C   1 
ATOM   3671 O  O   . PHE B 1 175 ? -27.366 26.857  17.167  1.00 30.96  ? 175 PHE B O   1 
ATOM   3672 C  CB  . PHE B 1 175 ? -25.473 24.971  16.054  1.00 23.44  ? 175 PHE B CB  1 
ATOM   3673 C  CG  . PHE B 1 175 ? -26.059 23.698  16.573  1.00 22.33  ? 175 PHE B CG  1 
ATOM   3674 C  CD1 . PHE B 1 175 ? -26.359 22.652  15.699  1.00 22.17  ? 175 PHE B CD1 1 
ATOM   3675 C  CD2 . PHE B 1 175 ? -26.465 23.601  17.889  1.00 20.27  ? 175 PHE B CD2 1 
ATOM   3676 C  CE1 . PHE B 1 175 ? -26.931 21.476  16.160  1.00 25.54  ? 175 PHE B CE1 1 
ATOM   3677 C  CE2 . PHE B 1 175 ? -26.976 22.412  18.368  1.00 24.00  ? 175 PHE B CE2 1 
ATOM   3678 C  CZ  . PHE B 1 175 ? -27.268 21.371  17.490  1.00 22.34  ? 175 PHE B CZ  1 
ATOM   3679 N  N   A THR B 1 176 ? -28.366 27.173  15.176  0.50 21.04  ? 176 THR B N   1 
ATOM   3680 N  N   B THR B 1 176 ? -28.437 27.064  15.180  0.50 23.99  ? 176 THR B N   1 
ATOM   3681 C  CA  A THR B 1 176 ? -29.442 27.989  15.658  0.50 21.44  ? 176 THR B CA  1 
ATOM   3682 C  CA  B THR B 1 176 ? -29.468 27.949  15.635  0.50 24.83  ? 176 THR B CA  1 
ATOM   3683 C  C   A THR B 1 176 ? -30.587 27.086  16.107  0.50 19.38  ? 176 THR B C   1 
ATOM   3684 C  C   B THR B 1 176 ? -30.659 27.098  16.043  0.50 20.96  ? 176 THR B C   1 
ATOM   3685 O  O   A THR B 1 176 ? -30.737 25.936  15.652  0.50 19.96  ? 176 THR B O   1 
ATOM   3686 O  O   B THR B 1 176 ? -30.866 25.980  15.539  0.50 20.70  ? 176 THR B O   1 
ATOM   3687 C  CB  A THR B 1 176 ? -29.796 28.991  14.560  0.50 22.84  ? 176 THR B CB  1 
ATOM   3688 C  CB  B THR B 1 176 ? -29.783 28.961  14.533  0.50 26.30  ? 176 THR B CB  1 
ATOM   3689 O  OG1 A THR B 1 176 ? -29.891 28.330  13.290  0.50 21.55  ? 176 THR B OG1 1 
ATOM   3690 O  OG1 B THR B 1 176 ? -30.551 29.993  15.149  0.50 38.29  ? 176 THR B OG1 1 
ATOM   3691 C  CG2 A THR B 1 176 ? -28.732 30.063  14.465  0.50 26.88  ? 176 THR B CG2 1 
ATOM   3692 C  CG2 B THR B 1 176 ? -30.534 28.336  13.365  0.50 25.50  ? 176 THR B CG2 1 
ATOM   3693 N  N   . ASN B 1 177 ? -31.424 27.660  16.974  1.00 22.78  ? 177 ASN B N   1 
ATOM   3694 C  CA  . ASN B 1 177 ? -32.700 27.130  17.386  1.00 21.47  ? 177 ASN B CA  1 
ATOM   3695 C  C   . ASN B 1 177 ? -32.598 25.801  18.124  1.00 21.86  ? 177 ASN B C   1 
ATOM   3696 O  O   . ASN B 1 177 ? -33.530 25.022  18.143  1.00 23.49  ? 177 ASN B O   1 
ATOM   3697 C  CB  . ASN B 1 177 ? -33.580 27.027  16.162  1.00 20.36  ? 177 ASN B CB  1 
ATOM   3698 C  CG  . ASN B 1 177 ? -33.881 28.397  15.557  1.00 20.17  ? 177 ASN B CG  1 
ATOM   3699 O  OD1 . ASN B 1 177 ? -34.590 29.193  16.141  1.00 23.20  ? 177 ASN B OD1 1 
ATOM   3700 N  ND2 . ASN B 1 177 ? -33.356 28.646  14.378  1.00 21.38  ? 177 ASN B ND2 1 
ATOM   3701 N  N   . PHE B 1 178 ? -31.458 25.556  18.752  1.00 20.91  ? 178 PHE B N   1 
ATOM   3702 C  CA  . PHE B 1 178 ? -31.332 24.353  19.541  1.00 21.27  ? 178 PHE B CA  1 
ATOM   3703 C  C   . PHE B 1 178 ? -31.829 24.673  20.952  1.00 18.48  ? 178 PHE B C   1 
ATOM   3704 O  O   . PHE B 1 178 ? -31.409 25.628  21.593  1.00 19.71  ? 178 PHE B O   1 
ATOM   3705 C  CB  . PHE B 1 178 ? -29.903 23.826  19.579  1.00 19.48  ? 178 PHE B CB  1 
ATOM   3706 C  CG  . PHE B 1 178 ? -29.800 22.595  20.459  1.00 19.35  ? 178 PHE B CG  1 
ATOM   3707 C  CD1 . PHE B 1 178 ? -30.242 21.358  19.978  1.00 19.80  ? 178 PHE B CD1 1 
ATOM   3708 C  CD2 . PHE B 1 178 ? -29.402 22.692  21.805  1.00 16.75  ? 178 PHE B CD2 1 
ATOM   3709 C  CE1 . PHE B 1 178 ? -30.129 20.235  20.770  1.00 21.46  ? 178 PHE B CE1 1 
ATOM   3710 C  CE2 . PHE B 1 178 ? -29.325 21.546  22.598  1.00 14.44  ? 178 PHE B CE2 1 
ATOM   3711 C  CZ  . PHE B 1 178 ? -29.719 20.346  22.096  1.00 16.65  ? 178 PHE B CZ  1 
ATOM   3712 N  N   . ASP B 1 179 ? -32.686 23.802  21.470  1.00 17.28  ? 179 ASP B N   1 
ATOM   3713 C  CA  . ASP B 1 179 ? -33.305 24.014  22.782  1.00 16.00  ? 179 ASP B CA  1 
ATOM   3714 C  C   . ASP B 1 179 ? -32.647 23.121  23.835  1.00 14.28  ? 179 ASP B C   1 
ATOM   3715 O  O   . ASP B 1 179 ? -32.880 21.906  23.886  1.00 15.64  ? 179 ASP B O   1 
ATOM   3716 C  CB  . ASP B 1 179 ? -34.814 23.684  22.682  1.00 18.56  ? 179 ASP B CB  1 
ATOM   3717 C  CG  . ASP B 1 179 ? -35.591 24.039  23.932  1.00 21.45  ? 179 ASP B CG  1 
ATOM   3718 O  OD1 . ASP B 1 179 ? -34.982 24.263  25.019  1.00 18.12  ? 179 ASP B OD1 1 
ATOM   3719 O  OD2 . ASP B 1 179 ? -36.790 24.201  23.799  1.00 28.08  ? 179 ASP B OD2 1 
ATOM   3720 N  N   . PRO B 1 180 ? -31.867 23.709  24.767  1.00 13.14  ? 180 PRO B N   1 
ATOM   3721 C  CA  . PRO B 1 180 ? -31.147 22.882  25.737  1.00 13.17  ? 180 PRO B CA  1 
ATOM   3722 C  C   . PRO B 1 180 ? -32.032 22.253  26.801  1.00 13.13  ? 180 PRO B C   1 
ATOM   3723 O  O   . PRO B 1 180 ? -31.595 21.375  27.523  1.00 12.10  ? 180 PRO B O   1 
ATOM   3724 C  CB  . PRO B 1 180 ? -30.148 23.909  26.345  1.00 15.16  ? 180 PRO B CB  1 
ATOM   3725 C  CG  . PRO B 1 180 ? -30.810 25.263  26.201  1.00 15.41  ? 180 PRO B CG  1 
ATOM   3726 C  CD  . PRO B 1 180 ? -31.451 25.128  24.821  1.00 16.63  ? 180 PRO B CD  1 
ATOM   3727 N  N   . ARG B 1 181 ? -33.310 22.661  26.837  1.00 12.51  ? 181 ARG B N   1 
ATOM   3728 C  CA  . ARG B 1 181 ? -34.169 21.990  27.805  1.00 12.25  ? 181 ARG B CA  1 
ATOM   3729 C  C   . ARG B 1 181 ? -34.274 20.518  27.434  1.00 14.30  ? 181 ARG B C   1 
ATOM   3730 O  O   . ARG B 1 181 ? -34.608 19.724  28.307  1.00 17.32  ? 181 ARG B O   1 
ATOM   3731 C  CB  . ARG B 1 181 ? -35.574 22.604  27.767  1.00 14.88  ? 181 ARG B CB  1 
ATOM   3732 C  CG  . ARG B 1 181 ? -35.558 24.057  28.281  1.00 17.38  ? 181 ARG B CG  1 
ATOM   3733 C  CD  . ARG B 1 181 ? -36.866 24.801  28.301  1.00 20.78  ? 181 ARG B CD  1 
ATOM   3734 N  NE  . ARG B 1 181 ? -37.264 25.025  26.933  1.00 22.39  ? 181 ARG B NE  1 
ATOM   3735 C  CZ  . ARG B 1 181 ? -38.340 25.739  26.595  1.00 23.60  ? 181 ARG B CZ  1 
ATOM   3736 N  NH1 . ARG B 1 181 ? -39.212 26.141  27.529  1.00 27.92  ? 181 ARG B NH1 1 
ATOM   3737 N  NH2 . ARG B 1 181 ? -38.671 25.887  25.314  1.00 26.26  ? 181 ARG B NH2 1 
ATOM   3738 N  N   . GLY B 1 182 ? -34.042 20.171  26.154  1.00 14.16  ? 182 GLY B N   1 
ATOM   3739 C  CA  . GLY B 1 182 ? -34.102 18.761  25.731  1.00 16.50  ? 182 GLY B CA  1 
ATOM   3740 C  C   . GLY B 1 182 ? -32.979 17.886  26.287  1.00 16.27  ? 182 GLY B C   1 
ATOM   3741 O  O   . GLY B 1 182 ? -33.006 16.679  26.044  1.00 18.02  ? 182 GLY B O   1 
ATOM   3742 N  N   . LEU B 1 183 ? -32.069 18.456  27.052  1.00 14.16  ? 183 LEU B N   1 
ATOM   3743 C  CA  . LEU B 1 183 ? -30.921 17.718  27.553  1.00 13.15  ? 183 LEU B CA  1 
ATOM   3744 C  C   . LEU B 1 183 ? -31.074 17.455  29.053  1.00 12.82  ? 183 LEU B C   1 
ATOM   3745 O  O   . LEU B 1 183 ? -30.157 16.869  29.621  1.00 13.53  ? 183 LEU B O   1 
ATOM   3746 C  CB  . LEU B 1 183 ? -29.656 18.548  27.290  1.00 13.08  ? 183 LEU B CB  1 
ATOM   3747 C  CG  . LEU B 1 183 ? -29.265 18.632  25.791  1.00 16.83  ? 183 LEU B CG  1 
ATOM   3748 C  CD1 . LEU B 1 183 ? -28.034 19.481  25.614  1.00 18.94  ? 183 LEU B CD1 1 
ATOM   3749 C  CD2 . LEU B 1 183 ? -29.131 17.305  25.079  1.00 18.98  ? 183 LEU B CD2 1 
ATOM   3750 N  N   A LEU B 1 184 ? -32.079 18.061  29.683  0.50 14.00  ? 184 LEU B N   1 
ATOM   3751 N  N   B LEU B 1 184 ? -32.166 17.955  29.683  0.50 15.35  ? 184 LEU B N   1 
ATOM   3752 C  CA  A LEU B 1 184 ? -32.214 17.918  31.119  0.50 13.70  ? 184 LEU B CA  1 
ATOM   3753 C  CA  B LEU B 1 184 ? -32.301 17.951  31.141  0.50 15.99  ? 184 LEU B CA  1 
ATOM   3754 C  C   A LEU B 1 184 ? -32.905 16.582  31.460  0.50 12.66  ? 184 LEU B C   1 
ATOM   3755 C  C   B LEU B 1 184 ? -33.140 16.760  31.627  0.50 14.98  ? 184 LEU B C   1 
ATOM   3756 O  O   A LEU B 1 184 ? -33.589 15.977  30.583  0.50 16.13  ? 184 LEU B O   1 
ATOM   3757 O  O   B LEU B 1 184 ? -34.256 16.504  31.126  0.50 19.91  ? 184 LEU B O   1 
ATOM   3758 C  CB  A LEU B 1 184 ? -32.969 19.140  31.663  0.50 15.02  ? 184 LEU B CB  1 
ATOM   3759 C  CB  B LEU B 1 184 ? -33.050 19.187  31.640  0.50 15.25  ? 184 LEU B CB  1 
ATOM   3760 C  CG  A LEU B 1 184 ? -32.502 20.486  31.088  0.50 11.25  ? 184 LEU B CG  1 
ATOM   3761 C  CG  B LEU B 1 184 ? -32.454 20.573  31.444  0.50 12.24  ? 184 LEU B CG  1 
ATOM   3762 C  CD1 A LEU B 1 184 ? -33.301 21.680  31.606  0.50 11.85  ? 184 LEU B CD1 1 
ATOM   3763 C  CD1 B LEU B 1 184 ? -33.291 21.660  32.118  0.50 13.75  ? 184 LEU B CD1 1 
ATOM   3764 C  CD2 A LEU B 1 184 ? -31.003 20.711  31.369  0.50 10.21  ? 184 LEU B CD2 1 
ATOM   3765 C  CD2 B LEU B 1 184 ? -31.064 20.607  32.022  0.50 11.59  ? 184 LEU B CD2 1 
ATOM   3766 N  N   . PRO B 1 185 ? -32.719 16.105  32.716  1.00 12.52  ? 185 PRO B N   1 
ATOM   3767 C  CA  . PRO B 1 185 ? -33.448 14.957  33.287  1.00 13.28  ? 185 PRO B CA  1 
ATOM   3768 C  C   . PRO B 1 185 ? -34.726 15.583  33.934  1.00 20.09  ? 185 PRO B C   1 
ATOM   3769 O  O   . PRO B 1 185 ? -34.863 16.796  34.053  1.00 27.26  ? 185 PRO B O   1 
ATOM   3770 C  CB  . PRO B 1 185 ? -32.477 14.407  34.339  1.00 10.69  ? 185 PRO B CB  1 
ATOM   3771 C  CG  . PRO B 1 185 ? -31.812 15.701  34.831  1.00 10.85  ? 185 PRO B CG  1 
ATOM   3772 C  CD  . PRO B 1 185 ? -31.554 16.529  33.552  1.00 10.05  ? 185 PRO B CD  1 
ATOM   3773 N  N   . GLU B 1 186 ? -35.646 14.660  34.364  1.00 16.66  ? 186 GLU B N   1 
ATOM   3774 C  CA  . GLU B 1 186 ? -36.882 15.126  35.019  1.00 21.09  ? 186 GLU B CA  1 
ATOM   3775 C  C   . GLU B 1 186 ? -36.623 15.899  36.303  1.00 15.91  ? 186 GLU B C   1 
ATOM   3776 O  O   . GLU B 1 186 ? -37.245 16.966  36.576  1.00 19.31  ? 186 GLU B O   1 
ATOM   3777 C  CB  . GLU B 1 186 ? -37.703 13.961  35.539  1.00 29.33  ? 186 GLU B CB  1 
ATOM   3778 C  CG  . GLU B 1 186 ? -38.498 13.314  34.472  1.00 35.24  ? 186 GLU B CG  1 
ATOM   3779 C  CD  . GLU B 1 186 ? -39.166 12.049  34.989  1.00 28.38  ? 186 GLU B CD  1 
ATOM   3780 O  OE1 . GLU B 1 186 ? -39.689 11.297  34.131  1.00 33.69  ? 186 GLU B OE1 1 
ATOM   3781 O  OE2 . GLU B 1 186 ? -39.158 11.800  36.219  1.00 29.53  ? 186 GLU B OE2 1 
ATOM   3782 N  N   . SER B 1 187 ? -35.686 15.378  37.114  1.00 17.00  ? 187 SER B N   1 
ATOM   3783 C  CA  . SER B 1 187 ? -35.523 15.960  38.436  1.00 17.22  ? 187 SER B CA  1 
ATOM   3784 C  C   . SER B 1 187 ? -34.396 16.999  38.403  1.00 15.68  ? 187 SER B C   1 
ATOM   3785 O  O   . SER B 1 187 ? -33.355 16.764  37.724  1.00 14.36  ? 187 SER B O   1 
ATOM   3786 C  CB  . SER B 1 187 ? -35.067 14.911  39.407  1.00 20.50  ? 187 SER B CB  1 
ATOM   3787 O  OG  . SER B 1 187 ? -34.878 15.482  40.722  1.00 19.24  ? 187 SER B OG  1 
ATOM   3788 N  N   . LEU B 1 188 ? -34.560 18.099  39.115  1.00 15.69  ? 188 LEU B N   1 
ATOM   3789 C  CA  . LEU B 1 188 ? -33.472 19.083  39.376  1.00 14.79  ? 188 LEU B CA  1 
ATOM   3790 C  C   . LEU B 1 188 ? -32.905 18.952  40.775  1.00 13.34  ? 188 LEU B C   1 
ATOM   3791 O  O   . LEU B 1 188 ? -32.130 19.837  41.202  1.00 14.99  ? 188 LEU B O   1 
ATOM   3792 C  CB  . LEU B 1 188 ? -34.012 20.503  39.154  1.00 18.14  ? 188 LEU B CB  1 
ATOM   3793 C  CG  . LEU B 1 188 ? -34.415 20.832  37.726  1.00 18.93  ? 188 LEU B CG  1 
ATOM   3794 C  CD1 . LEU B 1 188 ? -34.912 22.298  37.667  1.00 23.25  ? 188 LEU B CD1 1 
ATOM   3795 C  CD2 . LEU B 1 188 ? -33.284 20.594  36.717  1.00 21.13  ? 188 LEU B CD2 1 
ATOM   3796 N  N   . ASP B 1 189 ? -33.016 17.816  41.444  1.00 12.24  ? 189 ASP B N   1 
ATOM   3797 C  CA  . ASP B 1 189 ? -32.237 17.586  42.679  1.00 13.60  ? 189 ASP B CA  1 
ATOM   3798 C  C   . ASP B 1 189 ? -30.721 17.575  42.337  1.00 10.42  ? 189 ASP B C   1 
ATOM   3799 O  O   . ASP B 1 189 ? -30.296 17.019  41.319  1.00 11.18  ? 189 ASP B O   1 
ATOM   3800 C  CB  . ASP B 1 189 ? -32.596 16.254  43.347  1.00 15.46  ? 189 ASP B CB  1 
ATOM   3801 C  CG  . ASP B 1 189 ? -34.039 16.144  43.935  1.00 20.50  ? 189 ASP B CG  1 
ATOM   3802 O  OD1 . ASP B 1 189 ? -34.626 17.192  44.122  1.00 26.92  ? 189 ASP B OD1 1 
ATOM   3803 O  OD2 . ASP B 1 189 ? -34.464 15.003  44.180  1.00 31.87  ? 189 ASP B OD2 1 
ATOM   3804 N  N   . TYR B 1 190 ? -29.979 18.185  43.221  1.00 9.21   ? 190 TYR B N   1 
ATOM   3805 C  CA  . TYR B 1 190 ? -28.545 18.426  42.920  1.00 8.20   ? 190 TYR B CA  1 
ATOM   3806 C  C   . TYR B 1 190 ? -27.690 18.304  44.162  1.00 8.50   ? 190 TYR B C   1 
ATOM   3807 O  O   . TYR B 1 190 ? -28.110 18.478  45.310  1.00 9.24   ? 190 TYR B O   1 
ATOM   3808 C  CB  . TYR B 1 190 ? -28.408 19.797  42.211  1.00 9.86   ? 190 TYR B CB  1 
ATOM   3809 C  CG  . TYR B 1 190 ? -28.788 20.952  43.091  1.00 9.35   ? 190 TYR B CG  1 
ATOM   3810 C  CD1 . TYR B 1 190 ? -27.831 21.591  43.901  1.00 12.68  ? 190 TYR B CD1 1 
ATOM   3811 C  CD2 . TYR B 1 190 ? -30.085 21.478  43.034  1.00 10.83  ? 190 TYR B CD2 1 
ATOM   3812 C  CE1 . TYR B 1 190 ? -28.210 22.683  44.687  1.00 12.90  ? 190 TYR B CE1 1 
ATOM   3813 C  CE2 . TYR B 1 190 ? -30.464 22.561  43.831  1.00 10.87  ? 190 TYR B CE2 1 
ATOM   3814 C  CZ  . TYR B 1 190 ? -29.536 23.153  44.680  1.00 11.15  ? 190 TYR B CZ  1 
ATOM   3815 O  OH  . TYR B 1 190 ? -29.839 24.222  45.528  1.00 13.28  ? 190 TYR B OH  1 
ATOM   3816 N  N   . TRP B 1 191 ? -26.364 18.177  43.845  1.00 8.41   ? 191 TRP B N   1 
ATOM   3817 C  CA  . TRP B 1 191 ? -25.279 18.473  44.809  1.00 8.05   ? 191 TRP B CA  1 
ATOM   3818 C  C   . TRP B 1 191 ? -24.597 19.759  44.385  1.00 6.65   ? 191 TRP B C   1 
ATOM   3819 O  O   . TRP B 1 191 ? -24.556 20.101  43.227  1.00 7.66   ? 191 TRP B O   1 
ATOM   3820 C  CB  . TRP B 1 191 ? -24.291 17.337  44.836  1.00 8.54   ? 191 TRP B CB  1 
ATOM   3821 C  CG  . TRP B 1 191 ? -24.828 16.017  45.267  1.00 9.28   ? 191 TRP B CG  1 
ATOM   3822 C  CD1 . TRP B 1 191 ? -25.021 15.590  46.560  1.00 9.77   ? 191 TRP B CD1 1 
ATOM   3823 C  CD2 . TRP B 1 191 ? -25.043 14.869  44.426  1.00 8.89   ? 191 TRP B CD2 1 
ATOM   3824 N  NE1 . TRP B 1 191 ? -25.436 14.278  46.555  1.00 11.50  ? 191 TRP B NE1 1 
ATOM   3825 C  CE2 . TRP B 1 191 ? -25.502 13.802  45.261  1.00 8.74   ? 191 TRP B CE2 1 
ATOM   3826 C  CE3 . TRP B 1 191 ? -24.998 14.641  43.040  1.00 9.07   ? 191 TRP B CE3 1 
ATOM   3827 C  CZ2 . TRP B 1 191 ? -25.810 12.539  44.747  1.00 10.70  ? 191 TRP B CZ2 1 
ATOM   3828 C  CZ3 . TRP B 1 191 ? -25.267 13.370  42.515  1.00 10.18  ? 191 TRP B CZ3 1 
ATOM   3829 C  CH2 . TRP B 1 191 ? -25.572 12.334  43.385  1.00 10.51  ? 191 TRP B CH2 1 
ATOM   3830 N  N   . THR B 1 192 ? -24.041 20.464  45.392  1.00 7.55   ? 192 THR B N   1 
ATOM   3831 C  CA  . THR B 1 192 ? -23.296 21.675  45.039  1.00 7.03   ? 192 THR B CA  1 
ATOM   3832 C  C   . THR B 1 192 ? -22.074 21.894  45.903  1.00 7.78   ? 192 THR B C   1 
ATOM   3833 O  O   . THR B 1 192 ? -22.027 21.490  47.065  1.00 7.85   ? 192 THR B O   1 
ATOM   3834 C  CB  . THR B 1 192 ? -24.231 22.923  45.126  1.00 7.20   ? 192 THR B CB  1 
ATOM   3835 O  OG1 . THR B 1 192 ? -23.537 24.123  44.756  1.00 7.61   ? 192 THR B OG1 1 
ATOM   3836 C  CG2 . THR B 1 192 ? -24.802 23.115  46.505  1.00 8.64   ? 192 THR B CG2 1 
ATOM   3837 N  N   . TYR B 1 193 ? -21.006 22.470  45.290  1.00 7.51   ? 193 TYR B N   1 
ATOM   3838 C  CA  . TYR B 1 193 ? -19.795 22.768  46.055  1.00 7.18   ? 193 TYR B CA  1 
ATOM   3839 C  C   . TYR B 1 193 ? -19.021 23.803  45.266  1.00 6.14   ? 193 TYR B C   1 
ATOM   3840 O  O   . TYR B 1 193 ? -19.218 23.988  44.067  1.00 6.47   ? 193 TYR B O   1 
ATOM   3841 C  CB  . TYR B 1 193 ? -18.978 21.478  46.237  1.00 7.17   ? 193 TYR B CB  1 
ATOM   3842 C  CG  . TYR B 1 193 ? -18.293 21.023  44.977  1.00 6.43   ? 193 TYR B CG  1 
ATOM   3843 C  CD1 . TYR B 1 193 ? -18.956 20.299  43.990  1.00 6.98   ? 193 TYR B CD1 1 
ATOM   3844 C  CD2 . TYR B 1 193 ? -16.965 21.368  44.713  1.00 6.56   ? 193 TYR B CD2 1 
ATOM   3845 C  CE1 . TYR B 1 193 ? -18.317 19.911  42.812  1.00 6.39   ? 193 TYR B CE1 1 
ATOM   3846 C  CE2 . TYR B 1 193 ? -16.272 21.008  43.558  1.00 6.88   ? 193 TYR B CE2 1 
ATOM   3847 C  CZ  . TYR B 1 193 ? -16.967 20.331  42.602  1.00 6.60   ? 193 TYR B CZ  1 
ATOM   3848 O  OH  . TYR B 1 193 ? -16.348 19.952  41.454  1.00 6.54   ? 193 TYR B OH  1 
ATOM   3849 N  N   . PRO B 1 194 ? -18.112 24.479  45.975  1.00 6.49   ? 194 PRO B N   1 
ATOM   3850 C  CA  . PRO B 1 194 ? -17.272 25.492  45.295  1.00 7.00   ? 194 PRO B CA  1 
ATOM   3851 C  C   . PRO B 1 194 ? -16.065 24.796  44.594  1.00 6.18   ? 194 PRO B C   1 
ATOM   3852 O  O   . PRO B 1 194 ? -15.332 24.062  45.268  1.00 6.63   ? 194 PRO B O   1 
ATOM   3853 C  CB  . PRO B 1 194 ? -16.787 26.382  46.467  1.00 7.72   ? 194 PRO B CB  1 
ATOM   3854 C  CG  . PRO B 1 194 ? -16.798 25.460  47.642  1.00 8.02   ? 194 PRO B CG  1 
ATOM   3855 C  CD  . PRO B 1 194 ? -17.961 24.452  47.426  1.00 7.77   ? 194 PRO B CD  1 
ATOM   3856 N  N   . GLY B 1 195 ? -15.802 25.154  43.353  1.00 6.16   ? 195 GLY B N   1 
ATOM   3857 C  CA  . GLY B 1 195 ? -14.693 24.480  42.649  1.00 6.46   ? 195 GLY B CA  1 
ATOM   3858 C  C   . GLY B 1 195 ? -14.145 25.382  41.555  1.00 6.55   ? 195 GLY B C   1 
ATOM   3859 O  O   . GLY B 1 195 ? -14.003 26.598  41.684  1.00 6.51   ? 195 GLY B O   1 
ATOM   3860 N  N   . SER B 1 196 ? -13.756 24.715  40.490  1.00 6.67   ? 196 SER B N   1 
ATOM   3861 C  CA  . SER B 1 196 ? -12.892 25.352  39.469  1.00 7.61   ? 196 SER B CA  1 
ATOM   3862 C  C   . SER B 1 196 ? -13.336 24.946  38.059  1.00 6.36   ? 196 SER B C   1 
ATOM   3863 O  O   . SER B 1 196 ? -14.119 23.937  37.876  1.00 7.36   ? 196 SER B O   1 
ATOM   3864 C  CB  . SER B 1 196 ? -11.403 24.986  39.638  1.00 8.29   ? 196 SER B CB  1 
ATOM   3865 O  OG  . SER B 1 196 ? -11.214 23.599  39.241  1.00 7.93   ? 196 SER B OG  1 
ATOM   3866 N  N   . LEU B 1 197 ? -12.813 25.606  37.016  1.00 6.04   ? 197 LEU B N   1 
ATOM   3867 C  CA  . LEU B 1 197 ? -12.793 24.991  35.699  1.00 7.26   ? 197 LEU B CA  1 
ATOM   3868 C  C   . LEU B 1 197 ? -12.071 23.649  35.733  1.00 6.52   ? 197 LEU B C   1 
ATOM   3869 O  O   . LEU B 1 197 ? -11.109 23.490  36.524  1.00 7.27   ? 197 LEU B O   1 
ATOM   3870 C  CB  . LEU B 1 197 ? -12.048 25.911  34.724  1.00 7.53   ? 197 LEU B CB  1 
ATOM   3871 C  CG  . LEU B 1 197 ? -12.525 27.361  34.619  1.00 8.77   ? 197 LEU B CG  1 
ATOM   3872 C  CD1 . LEU B 1 197 ? -11.658 28.155  33.582  1.00 11.02  ? 197 LEU B CD1 1 
ATOM   3873 C  CD2 . LEU B 1 197 ? -13.986 27.507  34.288  1.00 10.51  ? 197 LEU B CD2 1 
ATOM   3874 N  N   . THR B 1 198 ? -12.466 22.724  34.875  1.00 6.75   ? 198 THR B N   1 
ATOM   3875 C  CA  . THR B 1 198 ? -11.768 21.454  34.816  1.00 7.69   ? 198 THR B CA  1 
ATOM   3876 C  C   . THR B 1 198 ? -10.761 21.355  33.641  1.00 7.32   ? 198 THR B C   1 
ATOM   3877 O  O   . THR B 1 198 ? -10.169 20.322  33.434  1.00 8.51   ? 198 THR B O   1 
ATOM   3878 C  CB  . THR B 1 198 ? -12.774 20.298  34.767  1.00 7.22   ? 198 THR B CB  1 
ATOM   3879 O  OG1 . THR B 1 198 ? -13.359 20.284  33.443  1.00 7.37   ? 198 THR B OG1 1 
ATOM   3880 C  CG2 . THR B 1 198 ? -13.795 20.267  35.884  1.00 6.73   ? 198 THR B CG2 1 
ATOM   3881 N  N   . THR B 1 199 ? -10.622 22.459  32.922  1.00 7.37   ? 199 THR B N   1 
ATOM   3882 C  CA  . THR B 1 199 ? -9.582  22.551  31.916  1.00 8.19   ? 199 THR B CA  1 
ATOM   3883 C  C   . THR B 1 199 ? -8.786  23.795  32.257  1.00 10.28  ? 199 THR B C   1 
ATOM   3884 O  O   . THR B 1 199 ? -9.250  24.753  32.889  1.00 10.11  ? 199 THR B O   1 
ATOM   3885 C  CB  . THR B 1 199 ? -10.152 22.795  30.520  1.00 10.36  ? 199 THR B CB  1 
ATOM   3886 O  OG1 . THR B 1 199 ? -11.057 23.925  30.492  1.00 13.67  ? 199 THR B OG1 1 
ATOM   3887 C  CG2 . THR B 1 199 ? -10.951 21.576  30.079  1.00 10.30  ? 199 THR B CG2 1 
ATOM   3888 N  N   . PRO B 1 200 ? -7.502  23.869  31.792  1.00 11.11  ? 200 PRO B N   1 
ATOM   3889 C  CA  . PRO B 1 200 ? -6.660  25.087  31.887  1.00 11.23  ? 200 PRO B CA  1 
ATOM   3890 C  C   . PRO B 1 200 ? -7.575  26.229  31.406  1.00 10.70  ? 200 PRO B C   1 
ATOM   3891 O  O   . PRO B 1 200 ? -8.243  26.202  30.333  1.00 11.03  ? 200 PRO B O   1 
ATOM   3892 C  CB  . PRO B 1 200 ? -5.545  24.769  30.848  1.00 12.16  ? 200 PRO B CB  1 
ATOM   3893 C  CG  . PRO B 1 200 ? -5.282  23.323  31.107  1.00 11.41  ? 200 PRO B CG  1 
ATOM   3894 C  CD  . PRO B 1 200 ? -6.766  22.810  31.109  1.00 10.89  ? 200 PRO B CD  1 
ATOM   3895 N  N   . PRO B 1 201 ? -7.556  27.381  32.090  1.00 9.80   ? 201 PRO B N   1 
ATOM   3896 C  CA  . PRO B 1 201 ? -6.597  27.729  33.138  1.00 9.97   ? 201 PRO B CA  1 
ATOM   3897 C  C   . PRO B 1 201 ? -6.952  27.251  34.552  1.00 9.83   ? 201 PRO B C   1 
ATOM   3898 O  O   . PRO B 1 201 ? -6.278  27.660  35.524  1.00 11.40  ? 201 PRO B O   1 
ATOM   3899 C  CB  . PRO B 1 201 ? -6.631  29.275  33.074  1.00 10.99  ? 201 PRO B CB  1 
ATOM   3900 C  CG  . PRO B 1 201 ? -8.010  29.599  32.683  1.00 11.03  ? 201 PRO B CG  1 
ATOM   3901 C  CD  . PRO B 1 201 ? -8.277  28.558  31.638  1.00 10.61  ? 201 PRO B CD  1 
ATOM   3902 N  N   . LEU B 1 202 ? -7.993  26.415  34.706  1.00 8.76   ? 202 LEU B N   1 
ATOM   3903 C  CA  . LEU B 1 202 ? -8.254  25.825  36.018  1.00 9.17   ? 202 LEU B CA  1 
ATOM   3904 C  C   . LEU B 1 202 ? -8.671  26.845  37.072  1.00 12.88  ? 202 LEU B C   1 
ATOM   3905 O  O   . LEU B 1 202 ? -8.526  26.604  38.249  1.00 10.99  ? 202 LEU B O   1 
ATOM   3906 C  CB  . LEU B 1 202 ? -7.123  24.881  36.514  1.00 9.79   ? 202 LEU B CB  1 
ATOM   3907 C  CG  . LEU B 1 202 ? -6.789  23.767  35.514  1.00 12.03  ? 202 LEU B CG  1 
ATOM   3908 C  CD1 . LEU B 1 202 ? -5.460  23.066  35.947  1.00 19.47  ? 202 LEU B CD1 1 
ATOM   3909 C  CD2 . LEU B 1 202 ? -7.942  22.744  35.397  1.00 11.65  ? 202 LEU B CD2 1 
ATOM   3910 N  N   . ALA B 1 203 ? -9.199  27.985  36.589  1.00 9.91   ? 203 ALA B N   1 
ATOM   3911 C  CA  . ALA B 1 203 ? -9.520  29.119  37.485  1.00 8.98   ? 203 ALA B CA  1 
ATOM   3912 C  C   . ALA B 1 203 ? -10.539 28.644  38.536  1.00 7.51   ? 203 ALA B C   1 
ATOM   3913 O  O   . ALA B 1 203 ? -11.549 27.911  38.258  1.00 7.72   ? 203 ALA B O   1 
ATOM   3914 C  CB  . ALA B 1 203 ? -10.081 30.233  36.716  1.00 8.99   ? 203 ALA B CB  1 
ATOM   3915 N  N   . GLU B 1 204 ? -10.379 29.095  39.788  1.00 8.02   ? 204 GLU B N   1 
ATOM   3916 C  CA  . GLU B 1 204 ? -11.216 28.735  40.928  1.00 7.41   ? 204 GLU B CA  1 
ATOM   3917 C  C   . GLU B 1 204 ? -12.302 29.786  41.073  1.00 7.96   ? 204 GLU B C   1 
ATOM   3918 O  O   . GLU B 1 204 ? -12.456 30.470  42.045  1.00 8.44   ? 204 GLU B O   1 
ATOM   3919 C  CB  . GLU B 1 204 ? -10.318 28.650  42.188  1.00 8.79   ? 204 GLU B CB  1 
ATOM   3920 C  CG  . GLU B 1 204 ? -9.410  27.410  42.031  1.00 10.33  ? 204 GLU B CG  1 
ATOM   3921 C  CD  . GLU B 1 204 ? -8.500  27.133  43.225  1.00 12.04  ? 204 GLU B CD  1 
ATOM   3922 O  OE1 . GLU B 1 204 ? -8.172  28.116  43.985  1.00 13.18  ? 204 GLU B OE1 1 
ATOM   3923 O  OE2 . GLU B 1 204 ? -8.154  25.961  43.411  1.00 11.83  ? 204 GLU B OE2 1 
ATOM   3924 N  N   . CYS B 1 205 ? -13.237 29.623  40.111  1.00 8.22   ? 205 CYS B N   1 
ATOM   3925 C  CA  . CYS B 1 205 ? -14.277 30.672  39.904  1.00 6.60   ? 205 CYS B CA  1 
ATOM   3926 C  C   . CYS B 1 205 ? -15.706 30.060  39.750  1.00 6.24   ? 205 CYS B C   1 
ATOM   3927 O  O   . CYS B 1 205 ? -16.617 30.769  39.372  1.00 7.91   ? 205 CYS B O   1 
ATOM   3928 C  CB  . CYS B 1 205 ? -14.020 31.549  38.664  1.00 8.09   ? 205 CYS B CB  1 
ATOM   3929 S  SG  . CYS B 1 205 ? -13.934 30.556  37.132  1.00 8.36   ? 205 CYS B SG  1 
ATOM   3930 N  N   . VAL B 1 206 ? -15.802 28.769  40.044  1.00 6.04   ? 206 VAL B N   1 
ATOM   3931 C  CA  . VAL B 1 206 ? -17.058 28.028  39.689  1.00 6.28   ? 206 VAL B CA  1 
ATOM   3932 C  C   . VAL B 1 206 ? -17.778 27.586  40.931  1.00 6.34   ? 206 VAL B C   1 
ATOM   3933 O  O   . VAL B 1 206 ? -17.296 26.934  41.814  1.00 7.58   ? 206 VAL B O   1 
ATOM   3934 C  CB  . VAL B 1 206 ? -16.759 26.751  38.840  1.00 6.48   ? 206 VAL B CB  1 
ATOM   3935 C  CG1 . VAL B 1 206 ? -18.133 26.074  38.525  1.00 7.23   ? 206 VAL B CG1 1 
ATOM   3936 C  CG2 . VAL B 1 206 ? -16.030 27.120  37.510  1.00 7.77   ? 206 VAL B CG2 1 
ATOM   3937 N  N   . THR B 1 207 ? -19.118 27.880  40.944  1.00 6.73   ? 207 THR B N   1 
ATOM   3938 C  CA  . THR B 1 207 ? -20.064 27.140  41.794  1.00 7.06   ? 207 THR B CA  1 
ATOM   3939 C  C   . THR B 1 207 ? -20.611 25.960  40.972  1.00 6.06   ? 207 THR B C   1 
ATOM   3940 O  O   . THR B 1 207 ? -21.248 26.181  39.943  1.00 6.07   ? 207 THR B O   1 
ATOM   3941 C  CB  . THR B 1 207 ? -21.273 28.009  42.208  1.00 7.32   ? 207 THR B CB  1 
ATOM   3942 O  OG1 . THR B 1 207 ? -20.758 29.160  42.945  1.00 8.15   ? 207 THR B OG1 1 
ATOM   3943 C  CG2 . THR B 1 207 ? -22.233 27.255  43.131  1.00 9.83   ? 207 THR B CG2 1 
ATOM   3944 N  N   . TRP B 1 208 ? -20.248 24.772  41.427  1.00 6.11   ? 208 TRP B N   1 
ATOM   3945 C  CA  . TRP B 1 208 ? -20.726 23.575  40.696  1.00 7.27   ? 208 TRP B CA  1 
ATOM   3946 C  C   . TRP B 1 208 ? -22.109 23.191  41.215  1.00 6.62   ? 208 TRP B C   1 
ATOM   3947 O  O   . TRP B 1 208 ? -22.337 23.142  42.396  1.00 7.55   ? 208 TRP B O   1 
ATOM   3948 C  CB  . TRP B 1 208 ? -19.766 22.398  40.929  1.00 5.81   ? 208 TRP B CB  1 
ATOM   3949 C  CG  . TRP B 1 208 ? -18.607 22.497  39.967  1.00 5.90   ? 208 TRP B CG  1 
ATOM   3950 C  CD1 . TRP B 1 208 ? -17.375 23.087  40.169  1.00 5.96   ? 208 TRP B CD1 1 
ATOM   3951 C  CD2 . TRP B 1 208 ? -18.641 22.063  38.617  1.00 6.35   ? 208 TRP B CD2 1 
ATOM   3952 N  NE1 . TRP B 1 208 ? -16.664 23.065  38.995  1.00 7.31   ? 208 TRP B NE1 1 
ATOM   3953 C  CE2 . TRP B 1 208 ? -17.403 22.437  38.034  1.00 6.43   ? 208 TRP B CE2 1 
ATOM   3954 C  CE3 . TRP B 1 208 ? -19.621 21.421  37.824  1.00 6.41   ? 208 TRP B CE3 1 
ATOM   3955 C  CZ2 . TRP B 1 208 ? -17.091 22.174  36.703  1.00 7.21   ? 208 TRP B CZ2 1 
ATOM   3956 C  CZ3 . TRP B 1 208 ? -19.265 21.133  36.553  1.00 6.59   ? 208 TRP B CZ3 1 
ATOM   3957 C  CH2 . TRP B 1 208 ? -18.056 21.484  35.983  1.00 7.61   ? 208 TRP B CH2 1 
ATOM   3958 N  N   . ILE B 1 209 ? -22.989 22.772  40.270  1.00 7.31   ? 209 ILE B N   1 
ATOM   3959 C  CA  . ILE B 1 209 ? -24.343 22.268  40.576  1.00 7.29   ? 209 ILE B CA  1 
ATOM   3960 C  C   . ILE B 1 209 ? -24.419 20.981  39.738  1.00 6.47   ? 209 ILE B C   1 
ATOM   3961 O  O   . ILE B 1 209 ? -24.475 21.075  38.556  1.00 6.62   ? 209 ILE B O   1 
ATOM   3962 C  CB  . ILE B 1 209 ? -25.421 23.297  40.155  1.00 7.68   ? 209 ILE B CB  1 
ATOM   3963 C  CG1 . ILE B 1 209 ? -25.197 24.553  40.999  1.00 9.51   ? 209 ILE B CG1 1 
ATOM   3964 C  CG2 . ILE B 1 209 ? -26.849 22.695  40.412  1.00 9.41   ? 209 ILE B CG2 1 
ATOM   3965 C  CD1 . ILE B 1 209 ? -25.962 25.801  40.577  1.00 11.13  ? 209 ILE B CD1 1 
ATOM   3966 N  N   . VAL B 1 210 ? -24.367 19.860  40.424  1.00 7.20   ? 210 VAL B N   1 
ATOM   3967 C  CA  . VAL B 1 210 ? -24.352 18.569  39.709  1.00 6.77   ? 210 VAL B CA  1 
ATOM   3968 C  C   . VAL B 1 210 ? -25.686 17.861  39.958  1.00 6.63   ? 210 VAL B C   1 
ATOM   3969 O  O   . VAL B 1 210 ? -25.994 17.589  41.128  1.00 8.00   ? 210 VAL B O   1 
ATOM   3970 C  CB  . VAL B 1 210 ? -23.152 17.712  40.203  1.00 8.54   ? 210 VAL B CB  1 
ATOM   3971 C  CG1 . VAL B 1 210 ? -23.129 16.352  39.447  1.00 8.96   ? 210 VAL B CG1 1 
ATOM   3972 C  CG2 . VAL B 1 210 ? -21.817 18.421  39.891  1.00 9.27   ? 210 VAL B CG2 1 
ATOM   3973 N  N   . LEU B 1 211 ? -26.394 17.571  38.849  1.00 7.97   ? 211 LEU B N   1 
ATOM   3974 C  CA  . LEU B 1 211 ? -27.730 16.948  39.054  1.00 7.97   ? 211 LEU B CA  1 
ATOM   3975 C  C   . LEU B 1 211 ? -27.491 15.516  39.473  1.00 8.02   ? 211 LEU B C   1 
ATOM   3976 O  O   . LEU B 1 211 ? -26.680 14.752  38.942  1.00 7.81   ? 211 LEU B O   1 
ATOM   3977 C  CB  . LEU B 1 211 ? -28.535 17.044  37.766  1.00 10.07  ? 211 LEU B CB  1 
ATOM   3978 C  CG  . LEU B 1 211 ? -28.858 18.452  37.331  1.00 10.08  ? 211 LEU B CG  1 
ATOM   3979 C  CD1 . LEU B 1 211 ? -29.857 18.489  36.145  1.00 12.25  ? 211 LEU B CD1 1 
ATOM   3980 C  CD2 . LEU B 1 211 ? -29.395 19.382  38.463  1.00 11.28  ? 211 LEU B CD2 1 
ATOM   3981 N  N   . LYS B 1 212 ? -28.392 15.034  40.375  1.00 9.22   ? 212 LYS B N   1 
ATOM   3982 C  CA  . LYS B 1 212 ? -28.330 13.627  40.794  1.00 9.70   ? 212 LYS B CA  1 
ATOM   3983 C  C   . LYS B 1 212 ? -28.840 12.651  39.728  1.00 8.36   ? 212 LYS B C   1 
ATOM   3984 O  O   . LYS B 1 212 ? -28.293 11.562  39.571  1.00 10.59  ? 212 LYS B O   1 
ATOM   3985 C  CB  . LYS B 1 212 ? -29.149 13.327  42.053  1.00 11.47  ? 212 LYS B CB  1 
ATOM   3986 C  CG  . LYS B 1 212 ? -29.153 11.875  42.546  1.00 17.59  ? 212 LYS B CG  1 
ATOM   3987 C  CD  . LYS B 1 212 ? -29.978 11.560  43.789  1.00 24.72  ? 212 LYS B CD  1 
ATOM   3988 C  CE  . LYS B 1 212 ? -30.093 10.053  43.976  1.00 31.39  ? 212 LYS B CE  1 
ATOM   3989 N  NZ  . LYS B 1 212 ? -30.957 9.657   45.122  1.00 42.64  ? 212 LYS B NZ  1 
ATOM   3990 N  N   . GLU B 1 213 ? -29.845 13.054  38.971  1.00 9.30   ? 213 GLU B N   1 
ATOM   3991 C  CA  . GLU B 1 213 ? -30.436 12.147  37.969  1.00 10.34  ? 213 GLU B CA  1 
ATOM   3992 C  C   . GLU B 1 213 ? -29.614 12.232  36.680  1.00 8.91   ? 213 GLU B C   1 
ATOM   3993 O  O   . GLU B 1 213 ? -29.589 13.268  36.054  1.00 9.23   ? 213 GLU B O   1 
ATOM   3994 C  CB  . GLU B 1 213 ? -31.873 12.571  37.679  1.00 16.26  ? 213 GLU B CB  1 
ATOM   3995 C  CG  . GLU B 1 213 ? -32.637 11.503  36.829  1.00 28.40  ? 213 GLU B CG  1 
ATOM   3996 C  CD  . GLU B 1 213 ? -34.146 11.806  36.549  1.00 27.72  ? 213 GLU B CD  1 
ATOM   3997 O  OE1 . GLU B 1 213 ? -34.662 12.653  37.225  1.00 22.25  ? 213 GLU B OE1 1 
ATOM   3998 O  OE2 . GLU B 1 213 ? -34.732 11.225  35.584  1.00 45.82  ? 213 GLU B OE2 1 
ATOM   3999 N  N   . PRO B 1 214 ? -29.076 11.118  36.222  1.00 8.75   ? 214 PRO B N   1 
ATOM   4000 C  CA  . PRO B 1 214 ? -28.417 11.118  34.905  1.00 8.50   ? 214 PRO B CA  1 
ATOM   4001 C  C   . PRO B 1 214 ? -29.474 11.158  33.785  1.00 8.71   ? 214 PRO B C   1 
ATOM   4002 O  O   . PRO B 1 214 ? -30.663 10.792  33.992  1.00 13.64  ? 214 PRO B O   1 
ATOM   4003 C  CB  . PRO B 1 214 ? -27.716 9.767   34.844  1.00 10.52  ? 214 PRO B CB  1 
ATOM   4004 C  CG  . PRO B 1 214 ? -28.634 8.900   35.670  1.00 12.89  ? 214 PRO B CG  1 
ATOM   4005 C  CD  . PRO B 1 214 ? -29.023 9.788   36.874  1.00 10.16  ? 214 PRO B CD  1 
ATOM   4006 N  N   . ILE B 1 215 ? -29.057 11.578  32.570  1.00 8.84   ? 215 ILE B N   1 
ATOM   4007 C  CA  . ILE B 1 215 ? -29.875 11.363  31.381  1.00 8.94   ? 215 ILE B CA  1 
ATOM   4008 C  C   . ILE B 1 215 ? -29.325 10.095  30.710  1.00 8.16   ? 215 ILE B C   1 
ATOM   4009 O  O   . ILE B 1 215 ? -28.157 9.730   30.869  1.00 8.40   ? 215 ILE B O   1 
ATOM   4010 C  CB  . ILE B 1 215 ? -29.843 12.565  30.424  1.00 10.42  ? 215 ILE B CB  1 
ATOM   4011 C  CG1 . ILE B 1 215 ? -28.429 12.874  29.903  1.00 10.50  ? 215 ILE B CG1 1 
ATOM   4012 C  CG2 . ILE B 1 215 ? -30.496 13.820  31.022  1.00 11.61  ? 215 ILE B CG2 1 
ATOM   4013 C  CD1 . ILE B 1 215 ? -28.472 13.806  28.702  1.00 13.34  ? 215 ILE B CD1 1 
ATOM   4014 N  N   A SER B 1 216 ? -30.215 9.390   29.984  0.50 9.31   ? 216 SER B N   1 
ATOM   4015 N  N   B SER B 1 216 ? -30.193 9.419   29.952  0.50 9.59   ? 216 SER B N   1 
ATOM   4016 C  CA  A SER B 1 216 ? -29.840 8.250   29.148  0.50 9.83   ? 216 SER B CA  1 
ATOM   4017 C  CA  B SER B 1 216 ? -29.784 8.259   29.178  0.50 9.94   ? 216 SER B CA  1 
ATOM   4018 C  C   A SER B 1 216 ? -29.610 8.713   27.728  0.50 9.89   ? 216 SER B C   1 
ATOM   4019 C  C   B SER B 1 216 ? -29.602 8.700   27.743  0.50 9.88   ? 216 SER B C   1 
ATOM   4020 O  O   A SER B 1 216 ? -30.467 9.395   27.148  0.50 10.19  ? 216 SER B O   1 
ATOM   4021 O  O   B SER B 1 216 ? -30.423 9.448   27.197  0.50 10.05  ? 216 SER B O   1 
ATOM   4022 C  CB  A SER B 1 216 ? -30.901 7.165   29.170  0.50 11.35  ? 216 SER B CB  1 
ATOM   4023 C  CB  B SER B 1 216 ? -30.809 7.147   29.354  0.50 12.34  ? 216 SER B CB  1 
ATOM   4024 O  OG  A SER B 1 216 ? -31.036 6.624   30.466  0.50 13.77  ? 216 SER B OG  1 
ATOM   4025 O  OG  B SER B 1 216 ? -30.575 6.031   28.510  0.50 15.36  ? 216 SER B OG  1 
ATOM   4026 N  N   . VAL B 1 217 ? -28.506 8.215   27.143  1.00 8.94   ? 217 VAL B N   1 
ATOM   4027 C  CA  . VAL B 1 217 ? -28.194 8.404   25.719  1.00 8.65   ? 217 VAL B CA  1 
ATOM   4028 C  C   . VAL B 1 217 ? -27.953 7.028   25.130  1.00 8.47   ? 217 VAL B C   1 
ATOM   4029 O  O   . VAL B 1 217 ? -27.631 6.107   25.846  1.00 9.37   ? 217 VAL B O   1 
ATOM   4030 C  CB  . VAL B 1 217 ? -27.010 9.339   25.482  1.00 9.77   ? 217 VAL B CB  1 
ATOM   4031 C  CG1 . VAL B 1 217 ? -27.319 10.716  26.142  1.00 11.13  ? 217 VAL B CG1 1 
ATOM   4032 C  CG2 . VAL B 1 217 ? -25.731 8.698   25.987  1.00 11.58  ? 217 VAL B CG2 1 
ATOM   4033 N  N   . SER B 1 218 ? -28.152 6.895   23.814  1.00 8.67   ? 218 SER B N   1 
ATOM   4034 C  CA  . SER B 1 218 ? -27.936 5.573   23.257  1.00 9.97   ? 218 SER B CA  1 
ATOM   4035 C  C   . SER B 1 218 ? -26.466 5.323   22.951  1.00 9.33   ? 218 SER B C   1 
ATOM   4036 O  O   . SER B 1 218 ? -25.627 6.241   22.802  1.00 9.70   ? 218 SER B O   1 
ATOM   4037 C  CB  . SER B 1 218 ? -28.780 5.358   22.024  1.00 11.55  ? 218 SER B CB  1 
ATOM   4038 O  OG  . SER B 1 218 ? -28.347 6.254   21.041  1.00 11.70  ? 218 SER B OG  1 
ATOM   4039 N  N   A SER B 1 219 ? -26.244 4.034   22.774  0.50 10.04  ? 219 SER B N   1 
ATOM   4040 N  N   B SER B 1 219 ? -26.126 4.044   22.793  0.50 11.82  ? 219 SER B N   1 
ATOM   4041 C  CA  A SER B 1 219 ? -24.929 3.647   22.357  0.50 10.74  ? 219 SER B CA  1 
ATOM   4042 C  CA  B SER B 1 219 ? -24.796 3.692   22.333  0.50 11.91  ? 219 SER B CA  1 
ATOM   4043 C  C   A SER B 1 219 ? -24.569 4.301   21.029  0.50 11.33  ? 219 SER B C   1 
ATOM   4044 C  C   B SER B 1 219 ? -24.496 4.338   20.985  0.50 12.74  ? 219 SER B C   1 
ATOM   4045 O  O   A SER B 1 219 ? -23.458 4.790   20.869  0.50 11.87  ? 219 SER B O   1 
ATOM   4046 O  O   B SER B 1 219 ? -23.373 4.811   20.763  0.50 13.41  ? 219 SER B O   1 
ATOM   4047 C  CB  A SER B 1 219 ? -24.753 2.161   22.343  0.50 11.08  ? 219 SER B CB  1 
ATOM   4048 C  CB  B SER B 1 219 ? -24.570 2.188   22.310  0.50 14.36  ? 219 SER B CB  1 
ATOM   4049 O  OG  A SER B 1 219 ? -25.591 1.586   21.358  0.50 11.71  ? 219 SER B OG  1 
ATOM   4050 O  OG  B SER B 1 219 ? -23.200 1.849   22.100  0.50 16.81  ? 219 SER B OG  1 
ATOM   4051 N  N   . GLU B 1 220 ? -25.479 4.466   20.098  1.00 12.13  ? 220 GLU B N   1 
ATOM   4052 C  CA  . GLU B 1 220 ? -25.225 5.110   18.832  1.00 12.08  ? 220 GLU B CA  1 
ATOM   4053 C  C   . GLU B 1 220 ? -24.899 6.589   18.987  1.00 11.62  ? 220 GLU B C   1 
ATOM   4054 O  O   . GLU B 1 220 ? -24.008 7.089   18.316  1.00 14.15  ? 220 GLU B O   1 
ATOM   4055 C  CB  . GLU B 1 220 ? -26.395 4.967   17.882  1.00 17.13  ? 220 GLU B CB  1 
ATOM   4056 C  CG  . GLU B 1 220 ? -26.603 3.511   17.481  1.00 22.41  ? 220 GLU B CG  1 
ATOM   4057 C  CD  . GLU B 1 220 ? -27.471 2.668   18.413  1.00 23.16  ? 220 GLU B CD  1 
ATOM   4058 O  OE1 . GLU B 1 220 ? -27.941 3.139   19.463  1.00 21.59  ? 220 GLU B OE1 1 
ATOM   4059 O  OE2 . GLU B 1 220 ? -27.816 1.576   18.014  1.00 34.66  ? 220 GLU B OE2 1 
ATOM   4060 N  N   . GLN B 1 221 ? -25.551 7.285   19.921  1.00 10.50  ? 221 GLN B N   1 
ATOM   4061 C  CA  . GLN B 1 221 ? -25.256 8.686   20.178  1.00 10.57  ? 221 GLN B CA  1 
ATOM   4062 C  C   . GLN B 1 221 ? -23.812 8.878   20.706  1.00 10.24  ? 221 GLN B C   1 
ATOM   4063 O  O   . GLN B 1 221 ? -23.029 9.701   20.195  1.00 11.50  ? 221 GLN B O   1 
ATOM   4064 C  CB  . GLN B 1 221 ? -26.321 9.236   21.132  1.00 11.34  ? 221 GLN B CB  1 
ATOM   4065 C  CG  . GLN B 1 221 ? -27.655 9.361   20.414  1.00 11.41  ? 221 GLN B CG  1 
ATOM   4066 C  CD  . GLN B 1 221 ? -28.703 9.944   21.340  1.00 11.25  ? 221 GLN B CD  1 
ATOM   4067 O  OE1 . GLN B 1 221 ? -28.855 9.563   22.526  1.00 10.22  ? 221 GLN B OE1 1 
ATOM   4068 N  NE2 . GLN B 1 221 ? -29.486 10.813  20.734  1.00 12.78  ? 221 GLN B NE2 1 
ATOM   4069 N  N   A VAL B 1 222 ? -23.468 8.054   21.694  0.50 11.06  ? 222 VAL B N   1 
ATOM   4070 N  N   B VAL B 1 222 ? -23.416 8.073   21.707  0.50 11.46  ? 222 VAL B N   1 
ATOM   4071 C  CA  A VAL B 1 222 ? -22.141 8.233   22.255  0.50 9.94   ? 222 VAL B CA  1 
ATOM   4072 C  CA  B VAL B 1 222 ? -22.059 8.208   22.253  0.50 11.75  ? 222 VAL B CA  1 
ATOM   4073 C  C   A VAL B 1 222 ? -21.046 7.797   21.270  0.50 12.20  ? 222 VAL B C   1 
ATOM   4074 C  C   B VAL B 1 222 ? -21.007 7.826   21.206  0.50 12.67  ? 222 VAL B C   1 
ATOM   4075 O  O   A VAL B 1 222 ? -19.945 8.383   21.259  0.50 12.42  ? 222 VAL B O   1 
ATOM   4076 O  O   B VAL B 1 222 ? -19.895 8.403   21.118  0.50 12.09  ? 222 VAL B O   1 
ATOM   4077 C  CB  A VAL B 1 222 ? -22.001 7.689   23.690  0.50 11.30  ? 222 VAL B CB  1 
ATOM   4078 C  CB  B VAL B 1 222 ? -21.853 7.430   23.569  0.50 14.71  ? 222 VAL B CB  1 
ATOM   4079 C  CG1 A VAL B 1 222 ? -21.919 6.170   23.719  0.50 11.62  ? 222 VAL B CG1 1 
ATOM   4080 C  CG1 B VAL B 1 222 ? -20.365 7.307   23.903  0.50 19.76  ? 222 VAL B CG1 1 
ATOM   4081 C  CG2 A VAL B 1 222 ? -20.797 8.332   24.404  0.50 10.79  ? 222 VAL B CG2 1 
ATOM   4082 C  CG2 B VAL B 1 222 ? -22.577 8.116   24.716  0.50 16.46  ? 222 VAL B CG2 1 
ATOM   4083 N  N   . LEU B 1 223 ? -21.345 6.847   20.377  1.00 12.04  ? 223 LEU B N   1 
ATOM   4084 C  CA  . LEU B 1 223 ? -20.403 6.441   19.380  1.00 13.96  ? 223 LEU B CA  1 
ATOM   4085 C  C   . LEU B 1 223 ? -20.106 7.601   18.452  1.00 11.54  ? 223 LEU B C   1 
ATOM   4086 O  O   . LEU B 1 223 ? -18.938 7.755   18.049  1.00 13.93  ? 223 LEU B O   1 
ATOM   4087 C  CB  . LEU B 1 223 ? -20.934 5.201   18.650  1.00 17.72  ? 223 LEU B CB  1 
ATOM   4088 C  CG  . LEU B 1 223 ? -20.748 3.919   19.487  1.00 25.06  ? 223 LEU B CG  1 
ATOM   4089 C  CD1 . LEU B 1 223 ? -21.519 2.734   18.910  1.00 30.29  ? 223 LEU B CD1 1 
ATOM   4090 C  CD2 . LEU B 1 223 ? -19.278 3.542   19.563  1.00 29.37  ? 223 LEU B CD2 1 
ATOM   4091 N  N   . LYS B 1 224 ? -21.060 8.473   18.171  1.00 12.13  ? 224 LYS B N   1 
ATOM   4092 C  CA  . LYS B 1 224 ? -20.808 9.636   17.325  1.00 15.38  ? 224 LYS B CA  1 
ATOM   4093 C  C   . LYS B 1 224 ? -19.876 10.643  18.001  1.00 12.06  ? 224 LYS B C   1 
ATOM   4094 O  O   . LYS B 1 224 ? -19.061 11.244  17.315  1.00 13.41  ? 224 LYS B O   1 
ATOM   4095 C  CB  . LYS B 1 224 ? -22.126 10.228  16.837  1.00 23.76  ? 224 LYS B CB  1 
ATOM   4096 C  CG  . LYS B 1 224 ? -22.793 9.291   15.830  1.00 24.95  ? 224 LYS B CG  1 
ATOM   4097 C  CD  . LYS B 1 224 ? -24.091 9.741   15.267  1.00 37.19  ? 224 LYS B CD  1 
ATOM   4098 C  CE  . LYS B 1 224 ? -24.487 9.031   13.978  1.00 44.86  ? 224 LYS B CE  1 
ATOM   4099 N  NZ  . LYS B 1 224 ? -23.738 9.624   12.821  1.00 46.96  ? 224 LYS B NZ  1 
ATOM   4100 N  N   . PHE B 1 225 ? -19.983 10.840  19.320  1.00 10.75  ? 225 PHE B N   1 
ATOM   4101 C  CA  . PHE B 1 225 ? -19.017 11.685  20.052  1.00 10.84  ? 225 PHE B CA  1 
ATOM   4102 C  C   . PHE B 1 225 ? -17.632 11.118  19.808  1.00 10.36  ? 225 PHE B C   1 
ATOM   4103 O  O   . PHE B 1 225 ? -16.714 11.889  19.568  1.00 12.13  ? 225 PHE B O   1 
ATOM   4104 C  CB  . PHE B 1 225 ? -19.249 11.589  21.568  1.00 11.70  ? 225 PHE B CB  1 
ATOM   4105 C  CG  . PHE B 1 225 ? -20.431 12.336  22.144  1.00 10.17  ? 225 PHE B CG  1 
ATOM   4106 C  CD1 . PHE B 1 225 ? -21.352 12.957  21.315  1.00 13.53  ? 225 PHE B CD1 1 
ATOM   4107 C  CD2 . PHE B 1 225 ? -20.621 12.417  23.513  1.00 11.74  ? 225 PHE B CD2 1 
ATOM   4108 C  CE1 . PHE B 1 225 ? -22.435 13.642  21.844  1.00 15.64  ? 225 PHE B CE1 1 
ATOM   4109 C  CE2 . PHE B 1 225 ? -21.704 13.102  24.041  1.00 12.36  ? 225 PHE B CE2 1 
ATOM   4110 C  CZ  . PHE B 1 225 ? -22.609 13.713  23.205  1.00 13.63  ? 225 PHE B CZ  1 
ATOM   4111 N  N   . ARG B 1 226 ? -17.502 9.785   19.848  1.00 10.28  ? 226 ARG B N   1 
ATOM   4112 C  CA  . ARG B 1 226 ? -16.173 9.171   19.800  1.00 10.79  ? 226 ARG B CA  1 
ATOM   4113 C  C   . ARG B 1 226 ? -15.564 9.109   18.380  1.00 10.57  ? 226 ARG B C   1 
ATOM   4114 O  O   . ARG B 1 226 ? -14.358 8.761   18.242  1.00 12.39  ? 226 ARG B O   1 
ATOM   4115 C  CB  . ARG B 1 226 ? -16.231 7.735   20.336  1.00 11.08  ? 226 ARG B CB  1 
ATOM   4116 C  CG  . ARG B 1 226 ? -16.631 7.618   21.800  1.00 11.29  ? 226 ARG B CG  1 
ATOM   4117 C  CD  . ARG B 1 226 ? -16.625 6.152   22.205  1.00 15.73  ? 226 ARG B CD  1 
ATOM   4118 N  NE  . ARG B 1 226 ? -17.083 6.025   23.592  1.00 11.77  ? 226 ARG B NE  1 
ATOM   4119 C  CZ  . ARG B 1 226 ? -17.937 5.115   24.047  1.00 11.75  ? 226 ARG B CZ  1 
ATOM   4120 N  NH1 . ARG B 1 226 ? -18.411 4.172   23.246  1.00 14.94  ? 226 ARG B NH1 1 
ATOM   4121 N  NH2 . ARG B 1 226 ? -18.288 5.157   25.312  1.00 13.35  ? 226 ARG B NH2 1 
ATOM   4122 N  N   . LYS B 1 227 ? -16.296 9.637   17.382  1.00 10.99  ? 227 LYS B N   1 
ATOM   4123 C  CA  . LYS B 1 227 ? -15.761 9.757   16.029  1.00 13.55  ? 227 LYS B CA  1 
ATOM   4124 C  C   . LYS B 1 227 ? -15.189 11.134  15.752  1.00 12.90  ? 227 LYS B C   1 
ATOM   4125 O  O   . LYS B 1 227 ? -14.534 11.320  14.719  1.00 15.25  ? 227 LYS B O   1 
ATOM   4126 C  CB  . LYS B 1 227 ? -16.885 9.488   15.014  1.00 15.87  ? 227 LYS B CB  1 
ATOM   4127 C  CG  . LYS B 1 227 ? -17.310 8.037   14.946  1.00 20.95  ? 227 LYS B CG  1 
ATOM   4128 C  CD  . LYS B 1 227 ? -18.378 7.813   13.833  1.00 25.88  ? 227 LYS B CD  1 
ATOM   4129 C  CE  . LYS B 1 227 ? -17.796 7.414   12.475  1.00 39.44  ? 227 LYS B CE  1 
ATOM   4130 N  NZ  . LYS B 1 227 ? -18.659 7.697   11.282  1.00 55.25  ? 227 LYS B NZ  1 
ATOM   4131 N  N   . LEU B 1 228 ? -15.416 12.066  16.677  1.00 11.90  ? 228 LEU B N   1 
ATOM   4132 C  CA  . LEU B 1 228 ? -14.725 13.322  16.541  1.00 15.37  ? 228 LEU B CA  1 
ATOM   4133 C  C   . LEU B 1 228 ? -13.217 13.103  16.665  1.00 14.05  ? 228 LEU B C   1 
ATOM   4134 O  O   . LEU B 1 228 ? -12.709 12.087  17.139  1.00 13.71  ? 228 LEU B O   1 
ATOM   4135 C  CB  . LEU B 1 228 ? -15.241 14.295  17.613  1.00 14.02  ? 228 LEU B CB  1 
ATOM   4136 C  CG  . LEU B 1 228 ? -16.684 14.764  17.421  1.00 13.73  ? 228 LEU B CG  1 
ATOM   4137 C  CD1 . LEU B 1 228 ? -17.146 15.396  18.734  1.00 13.80  ? 228 LEU B CD1 1 
ATOM   4138 C  CD2 . LEU B 1 228 ? -16.772 15.792  16.291  1.00 16.78  ? 228 LEU B CD2 1 
ATOM   4139 N  N   . ASN B 1 229 ? -12.465 14.156  16.294  1.00 16.74  ? 229 ASN B N   1 
ATOM   4140 C  CA  . ASN B 1 229 ? -11.005 14.177  16.323  1.00 16.98  ? 229 ASN B CA  1 
ATOM   4141 C  C   . ASN B 1 229 ? -10.460 15.375  17.095  1.00 17.97  ? 229 ASN B C   1 
ATOM   4142 O  O   . ASN B 1 229 ? -10.991 16.476  17.017  1.00 16.46  ? 229 ASN B O   1 
ATOM   4143 C  CB  . ASN B 1 229 ? -10.330 14.334  14.923  1.00 21.46  ? 229 ASN B CB  1 
ATOM   4144 C  CG  . ASN B 1 229 ? -10.383 13.117  14.008  1.00 23.11  ? 229 ASN B CG  1 
ATOM   4145 O  OD1 . ASN B 1 229 ? -9.681  13.087  12.987  1.00 29.01  ? 229 ASN B OD1 1 
ATOM   4146 N  ND2 . ASN B 1 229 ? -11.199 12.115  14.293  1.00 21.76  ? 229 ASN B ND2 1 
ATOM   4147 N  N   . PHE B 1 230 ? -9.468  15.048  17.908  1.00 18.20  ? 230 PHE B N   1 
ATOM   4148 C  CA  . PHE B 1 230 ? -8.629  16.061  18.591  1.00 16.64  ? 230 PHE B CA  1 
ATOM   4149 C  C   . PHE B 1 230 ? -7.775  16.852  17.602  1.00 19.02  ? 230 PHE B C   1 
ATOM   4150 O  O   . PHE B 1 230 ? -7.441  17.980  17.877  1.00 19.04  ? 230 PHE B O   1 
ATOM   4151 C  CB  . PHE B 1 230 ? -7.666  15.409  19.591  1.00 18.82  ? 230 PHE B CB  1 
ATOM   4152 C  CG  . PHE B 1 230 ? -8.210  14.848  20.888  1.00 16.65  ? 230 PHE B CG  1 
ATOM   4153 C  CD1 . PHE B 1 230 ? -8.928  15.635  21.760  1.00 15.23  ? 230 PHE B CD1 1 
ATOM   4154 C  CD2 . PHE B 1 230 ? -7.884  13.548  21.279  1.00 17.06  ? 230 PHE B CD2 1 
ATOM   4155 C  CE1 . PHE B 1 230 ? -9.359  15.142  23.008  1.00 16.04  ? 230 PHE B CE1 1 
ATOM   4156 C  CE2 . PHE B 1 230 ? -8.346  13.032  22.481  1.00 16.49  ? 230 PHE B CE2 1 
ATOM   4157 C  CZ  . PHE B 1 230 ? -9.103  13.817  23.360  1.00 17.37  ? 230 PHE B CZ  1 
ATOM   4158 N  N   . ASN B 1 231 ? -7.305  16.225  16.548  1.00 19.87  ? 231 ASN B N   1 
ATOM   4159 C  CA  . ASN B 1 231 ? -6.421  16.901  15.585  1.00 19.51  ? 231 ASN B CA  1 
ATOM   4160 C  C   . ASN B 1 231 ? -7.188  17.766  14.564  1.00 17.89  ? 231 ASN B C   1 
ATOM   4161 O  O   . ASN B 1 231 ? -8.401  17.770  14.504  1.00 20.08  ? 231 ASN B O   1 
ATOM   4162 C  CB  . ASN B 1 231 ? -5.642  15.813  14.860  1.00 23.29  ? 231 ASN B CB  1 
ATOM   4163 C  CG  . ASN B 1 231 ? -6.568  14.798  14.265  1.00 20.77  ? 231 ASN B CG  1 
ATOM   4164 O  OD1 . ASN B 1 231 ? -6.976  13.872  14.982  1.00 25.42  ? 231 ASN B OD1 1 
ATOM   4165 N  ND2 . ASN B 1 231 ? -6.898  14.994  12.986  1.00 22.21  ? 231 ASN B ND2 1 
ATOM   4166 N  N   . GLY B 1 232 ? -6.433  18.704  13.894  1.00 25.18  ? 232 GLY B N   1 
ATOM   4167 C  CA  . GLY B 1 232 ? -7.039  19.610  12.899  1.00 23.83  ? 232 GLY B CA  1 
ATOM   4168 C  C   . GLY B 1 232 ? -7.175  18.964  11.510  1.00 16.87  ? 232 GLY B C   1 
ATOM   4169 O  O   . GLY B 1 232 ? -6.545  17.989  11.340  1.00 20.63  ? 232 GLY B O   1 
ATOM   4170 N  N   . GLU B 1 233 ? -7.966  19.484  10.580  1.00 17.43  ? 233 GLU B N   1 
ATOM   4171 C  CA  . GLU B 1 233 ? -8.044  18.966  9.162   1.00 14.86  ? 233 GLU B CA  1 
ATOM   4172 C  C   . GLU B 1 233 ? -6.854  18.160  8.571   1.00 25.84  ? 233 GLU B C   1 
ATOM   4173 O  O   . GLU B 1 233 ? -7.177  17.291  7.761   1.00 33.59  ? 233 GLU B O   1 
ATOM   4174 C  CB  . GLU B 1 233 ? -8.718  19.865  8.127   1.00 17.06  ? 233 GLU B CB  1 
ATOM   4175 C  CG  . GLU B 1 233 ? -9.264  19.038  6.964   1.00 17.25  ? 233 GLU B CG  1 
ATOM   4176 C  CD  . GLU B 1 233 ? -10.119 19.868  6.020   1.00 26.84  ? 233 GLU B CD  1 
ATOM   4177 O  OE1 . GLU B 1 233 ? -10.458 21.014  6.384   1.00 28.88  ? 233 GLU B OE1 1 
ATOM   4178 O  OE2 . GLU B 1 233 ? -10.440 19.375  4.923   1.00 35.70  ? 233 GLU B OE2 1 
ATOM   4179 N  N   . GLY B 1 234 ? -5.545  18.316  8.852   1.00 38.40  ? 234 GLY B N   1 
ATOM   4180 C  CA  . GLY B 1 234 ? -4.749  17.159  8.378   1.00 37.20  ? 234 GLY B CA  1 
ATOM   4181 C  C   . GLY B 1 234 ? -3.403  16.719  8.989   1.00 43.42  ? 234 GLY B C   1 
ATOM   4182 O  O   . GLY B 1 234 ? -2.440  16.745  8.248   1.00 42.65  ? 234 GLY B O   1 
ATOM   4183 N  N   . GLU B 1 235 ? -3.338  16.295  10.292  1.00 37.88  ? 235 GLU B N   1 
ATOM   4184 C  CA  . GLU B 1 235 ? -2.179  15.685  11.001  1.00 40.92  ? 235 GLU B CA  1 
ATOM   4185 C  C   . GLU B 1 235 ? -2.526  14.262  11.462  1.00 20.44  ? 235 GLU B C   1 
ATOM   4186 O  O   . GLU B 1 235 ? -3.622  13.846  11.124  1.00 34.51  ? 235 GLU B O   1 
ATOM   4187 C  CB  . GLU B 1 235 ? -1.841  16.453  12.282  1.00 53.41  ? 235 GLU B CB  1 
ATOM   4188 C  CG  . GLU B 1 235 ? -1.016  17.720  12.032  1.00 62.48  ? 235 GLU B CG  1 
ATOM   4189 C  CD  . GLU B 1 235 ? 0.495   17.539  12.026  1.00 82.28  ? 235 GLU B CD  1 
ATOM   4190 O  OE1 . GLU B 1 235 ? 1.128   17.954  11.028  1.00 82.95  ? 235 GLU B OE1 1 
ATOM   4191 O  OE2 . GLU B 1 235 ? 1.035   17.006  13.029  1.00 96.00  ? 235 GLU B OE2 1 
ATOM   4192 N  N   . PRO B 1 236 ? -1.613  13.389  12.044  1.00 20.92  ? 236 PRO B N   1 
ATOM   4193 C  CA  . PRO B 1 236 ? -2.142  12.054  12.351  1.00 24.16  ? 236 PRO B CA  1 
ATOM   4194 C  C   . PRO B 1 236 ? -3.506  12.065  13.115  1.00 27.91  ? 236 PRO B C   1 
ATOM   4195 O  O   . PRO B 1 236 ? -3.747  12.892  14.039  1.00 33.41  ? 236 PRO B O   1 
ATOM   4196 C  CB  . PRO B 1 236 ? -0.954  11.423  13.126  1.00 22.75  ? 236 PRO B CB  1 
ATOM   4197 C  CG  . PRO B 1 236 ? 0.256   12.037  12.505  1.00 20.41  ? 236 PRO B CG  1 
ATOM   4198 C  CD  . PRO B 1 236 ? -0.175  13.491  12.338  1.00 21.46  ? 236 PRO B CD  1 
ATOM   4199 N  N   . GLU B 1 237 ? -4.361  11.124  12.772  1.00 24.98  ? 237 GLU B N   1 
ATOM   4200 C  CA  . GLU B 1 237 ? -5.674  11.070  13.348  1.00 25.58  ? 237 GLU B CA  1 
ATOM   4201 C  C   . GLU B 1 237 ? -5.726  10.577  14.752  1.00 25.07  ? 237 GLU B C   1 
ATOM   4202 O  O   . GLU B 1 237 ? -5.299  9.424   14.959  1.00 22.35  ? 237 GLU B O   1 
ATOM   4203 C  CB  . GLU B 1 237 ? -6.523  10.117  12.520  1.00 33.27  ? 237 GLU B CB  1 
ATOM   4204 C  CG  . GLU B 1 237 ? -7.963  10.166  12.936  1.00 33.84  ? 237 GLU B CG  1 
ATOM   4205 C  CD  . GLU B 1 237 ? -8.900  9.271   12.168  1.00 41.46  ? 237 GLU B CD  1 
ATOM   4206 O  OE1 . GLU B 1 237 ? -8.502  8.699   11.147  1.00 34.93  ? 237 GLU B OE1 1 
ATOM   4207 O  OE2 . GLU B 1 237 ? -10.035 9.242   12.576  1.00 44.82  ? 237 GLU B OE2 1 
ATOM   4208 N  N   A GLU B 1 238 ? -6.259  11.320  15.711  0.50 23.49  ? 238 GLU B N   1 
ATOM   4209 N  N   B GLU B 1 238 ? -6.317  11.330  15.673  0.50 20.92  ? 238 GLU B N   1 
ATOM   4210 C  CA  A GLU B 1 238 ? -6.327  10.863  17.106  0.50 22.47  ? 238 GLU B CA  1 
ATOM   4211 C  CA  B GLU B 1 238 ? -6.426  10.953  17.079  0.50 18.13  ? 238 GLU B CA  1 
ATOM   4212 C  C   A GLU B 1 238 ? -7.811  11.072  17.530  0.50 18.75  ? 238 GLU B C   1 
ATOM   4213 C  C   B GLU B 1 238 ? -7.899  11.153  17.484  0.50 21.20  ? 238 GLU B C   1 
ATOM   4214 O  O   A GLU B 1 238 ? -8.303  12.145  17.500  0.50 22.72  ? 238 GLU B O   1 
ATOM   4215 O  O   B GLU B 1 238 ? -8.385  12.234  17.512  0.50 28.90  ? 238 GLU B O   1 
ATOM   4216 C  CB  A GLU B 1 238 ? -5.236  11.547  18.009  0.50 22.36  ? 238 GLU B CB  1 
ATOM   4217 C  CB  B GLU B 1 238 ? -5.437  11.765  17.934  0.50 22.83  ? 238 GLU B CB  1 
ATOM   4218 C  CG  A GLU B 1 238 ? -3.770  10.989  17.938  0.50 18.35  ? 238 GLU B CG  1 
ATOM   4219 C  CG  B GLU B 1 238 ? -5.272  11.327  19.384  0.50 25.20  ? 238 GLU B CG  1 
ATOM   4220 C  CD  A GLU B 1 238 ? -2.798  11.740  18.851  0.50 19.84  ? 238 GLU B CD  1 
ATOM   4221 C  CD  B GLU B 1 238 ? -4.959  9.845   19.583  0.50 29.40  ? 238 GLU B CD  1 
ATOM   4222 O  OE1 A GLU B 1 238 ? -2.759  11.413  20.048  0.50 22.56  ? 238 GLU B OE1 1 
ATOM   4223 O  OE1 B GLU B 1 238 ? -4.848  9.092   18.590  0.50 30.61  ? 238 GLU B OE1 1 
ATOM   4224 O  OE2 A GLU B 1 238 ? -2.074  12.647  18.386  0.50 33.74  ? 238 GLU B OE2 1 
ATOM   4225 O  OE2 B GLU B 1 238 ? -4.763  9.432   20.736  0.50 28.13  ? 238 GLU B OE2 1 
ATOM   4226 N  N   A LEU B 1 239 ? -8.520  9.973   17.852  0.50 15.43  ? 239 LEU B N   1 
ATOM   4227 N  N   B LEU B 1 239 ? -8.613  10.027  17.679  0.50 16.15  ? 239 LEU B N   1 
ATOM   4228 C  CA  A LEU B 1 239 ? -9.951  10.113  18.166  0.50 13.26  ? 239 LEU B CA  1 
ATOM   4229 C  CA  B LEU B 1 239 ? -10.002 10.101  18.087  0.50 13.41  ? 239 LEU B CA  1 
ATOM   4230 C  C   A LEU B 1 239 ? -10.150 10.865  19.472  0.50 11.50  ? 239 LEU B C   1 
ATOM   4231 C  C   B LEU B 1 239 ? -10.102 10.921  19.379  0.50 11.72  ? 239 LEU B C   1 
ATOM   4232 O  O   A LEU B 1 239 ? -9.498  10.609  20.493  0.50 13.61  ? 239 LEU B O   1 
ATOM   4233 O  O   B LEU B 1 239 ? -9.275  10.847  20.289  0.50 13.19  ? 239 LEU B O   1 
ATOM   4234 C  CB  A LEU B 1 239 ? -10.627 8.729   18.250  0.50 11.89  ? 239 LEU B CB  1 
ATOM   4235 C  CB  B LEU B 1 239 ? -10.435 8.648   18.313  0.50 13.88  ? 239 LEU B CB  1 
ATOM   4236 C  CG  A LEU B 1 239 ? -10.600 7.958   16.921  0.50 10.98  ? 239 LEU B CG  1 
ATOM   4237 C  CG  B LEU B 1 239 ? -10.662 7.731   17.091  0.50 11.91  ? 239 LEU B CG  1 
ATOM   4238 C  CD1 A LEU B 1 239 ? -10.884 6.483   17.084  0.50 15.00  ? 239 LEU B CD1 1 
ATOM   4239 C  CD1 B LEU B 1 239 ? -9.345  7.330   16.329  0.50 11.25  ? 239 LEU B CD1 1 
ATOM   4240 C  CD2 A LEU B 1 239 ? -11.569 8.605   15.987  0.50 6.60   ? 239 LEU B CD2 1 
ATOM   4241 C  CD2 B LEU B 1 239 ? -11.394 6.530   17.640  0.50 11.70  ? 239 LEU B CD2 1 
ATOM   4242 N  N   . MET B 1 240 ? -11.119 11.772  19.414  1.00 11.70  ? 240 MET B N   1 
ATOM   4243 C  CA  . MET B 1 240 ? -11.446 12.569  20.599  1.00 11.63  ? 240 MET B CA  1 
ATOM   4244 C  C   . MET B 1 240 ? -12.230 11.672  21.565  1.00 10.46  ? 240 MET B C   1 
ATOM   4245 O  O   . MET B 1 240 ? -13.457 11.509  21.483  1.00 10.26  ? 240 MET B O   1 
ATOM   4246 C  CB  . MET B 1 240 ? -12.368 13.741  20.149  1.00 13.89  ? 240 MET B CB  1 
ATOM   4247 C  CG  . MET B 1 240 ? -12.645 14.754  21.315  1.00 13.24  ? 240 MET B CG  1 
ATOM   4248 S  SD  . MET B 1 240 ? -13.638 16.154  20.769  1.00 14.35  ? 240 MET B SD  1 
ATOM   4249 C  CE  . MET B 1 240 ? -12.322 17.195  20.114  1.00 15.42  ? 240 MET B CE  1 
ATOM   4250 N  N   . VAL B 1 241 ? -11.514 11.111  22.538  1.00 9.98   ? 241 VAL B N   1 
ATOM   4251 C  CA  . VAL B 1 241 ? -12.093 10.280  23.578  1.00 9.67   ? 241 VAL B CA  1 
ATOM   4252 C  C   . VAL B 1 241 ? -11.253 10.501  24.819  1.00 8.78   ? 241 VAL B C   1 
ATOM   4253 O  O   . VAL B 1 241 ? -10.096 10.957  24.768  1.00 9.39   ? 241 VAL B O   1 
ATOM   4254 C  CB  . VAL B 1 241 ? -12.035 8.765   23.238  1.00 9.57   ? 241 VAL B CB  1 
ATOM   4255 C  CG1 . VAL B 1 241 ? -12.824 8.409   22.037  1.00 10.79  ? 241 VAL B CG1 1 
ATOM   4256 C  CG2 . VAL B 1 241 ? -10.566 8.308   23.019  1.00 11.02  ? 241 VAL B CG2 1 
ATOM   4257 N  N   . ASP B 1 242 ? -11.838 10.263  26.002  1.00 7.90   ? 242 ASP B N   1 
ATOM   4258 C  CA  . ASP B 1 242 ? -11.140 10.434  27.261  1.00 7.94   ? 242 ASP B CA  1 
ATOM   4259 C  C   . ASP B 1 242 ? -10.713 11.851  27.504  1.00 7.51   ? 242 ASP B C   1 
ATOM   4260 O  O   . ASP B 1 242 ? -9.559  12.102  27.941  1.00 9.44   ? 242 ASP B O   1 
ATOM   4261 C  CB  . ASP B 1 242 ? -10.054 9.359   27.486  1.00 7.82   ? 242 ASP B CB  1 
ATOM   4262 C  CG  . ASP B 1 242 ? -10.629 7.970   27.592  1.00 7.75   ? 242 ASP B CG  1 
ATOM   4263 O  OD1 . ASP B 1 242 ? -11.674 7.791   28.284  1.00 8.28   ? 242 ASP B OD1 1 
ATOM   4264 O  OD2 . ASP B 1 242 ? -10.063 7.038   26.993  1.00 9.25   ? 242 ASP B OD2 1 
ATOM   4265 N  N   . ASN B 1 243 ? -11.566 12.780  27.240  1.00 6.95   ? 243 ASN B N   1 
ATOM   4266 C  CA  . ASN B 1 243 ? -11.336 14.193  27.439  1.00 8.37   ? 243 ASN B CA  1 
ATOM   4267 C  C   . ASN B 1 243 ? -11.897 14.658  28.793  1.00 8.26   ? 243 ASN B C   1 
ATOM   4268 O  O   . ASN B 1 243 ? -12.530 15.712  28.879  1.00 7.97   ? 243 ASN B O   1 
ATOM   4269 C  CB  . ASN B 1 243 ? -11.886 15.041  26.303  1.00 9.62   ? 243 ASN B CB  1 
ATOM   4270 C  CG  . ASN B 1 243 ? -13.339 14.794  26.021  1.00 9.31   ? 243 ASN B CG  1 
ATOM   4271 O  OD1 . ASN B 1 243 ? -14.024 14.011  26.686  1.00 9.34   ? 243 ASN B OD1 1 
ATOM   4272 N  ND2 . ASN B 1 243 ? -13.908 15.508  25.068  1.00 10.84  ? 243 ASN B ND2 1 
ATOM   4273 N  N   . TRP B 1 244 ? -11.592 13.895  29.841  1.00 8.11   ? 244 TRP B N   1 
ATOM   4274 C  CA  . TRP B 1 244 ? -12.031 14.195  31.194  1.00 7.13   ? 244 TRP B CA  1 
ATOM   4275 C  C   . TRP B 1 244 ? -10.823 14.295  32.122  1.00 7.54   ? 244 TRP B C   1 
ATOM   4276 O  O   . TRP B 1 244 ? -9.827  13.583  31.979  1.00 7.80   ? 244 TRP B O   1 
ATOM   4277 C  CB  . TRP B 1 244 ? -12.988 13.076  31.725  1.00 7.89   ? 244 TRP B CB  1 
ATOM   4278 C  CG  . TRP B 1 244 ? -12.473 11.682  31.559  1.00 7.84   ? 244 TRP B CG  1 
ATOM   4279 C  CD1 . TRP B 1 244 ? -12.559 10.927  30.422  1.00 7.31   ? 244 TRP B CD1 1 
ATOM   4280 C  CD2 . TRP B 1 244 ? -11.904 10.844  32.530  1.00 7.76   ? 244 TRP B CD2 1 
ATOM   4281 N  NE1 . TRP B 1 244 ? -12.069 9.670   30.646  1.00 7.26   ? 244 TRP B NE1 1 
ATOM   4282 C  CE2 . TRP B 1 244 ? -11.627 9.591   31.930  1.00 7.50   ? 244 TRP B CE2 1 
ATOM   4283 C  CE3 . TRP B 1 244 ? -11.589 10.991  33.901  1.00 7.34   ? 244 TRP B CE3 1 
ATOM   4284 C  CZ2 . TRP B 1 244 ? -11.072 8.532   32.623  1.00 8.20   ? 244 TRP B CZ2 1 
ATOM   4285 C  CZ3 . TRP B 1 244 ? -11.070 9.931   34.605  1.00 7.96   ? 244 TRP B CZ3 1 
ATOM   4286 C  CH2 . TRP B 1 244 ? -10.827 8.683   33.969  1.00 8.35   ? 244 TRP B CH2 1 
ATOM   4287 N  N   . ARG B 1 245 ? -10.972 15.155  33.118  1.00 7.09   ? 245 ARG B N   1 
ATOM   4288 C  CA  . ARG B 1 245 ? -10.008 15.309  34.191  1.00 7.19   ? 245 ARG B CA  1 
ATOM   4289 C  C   . ARG B 1 245 ? -10.429 14.454  35.347  1.00 6.74   ? 245 ARG B C   1 
ATOM   4290 O  O   . ARG B 1 245 ? -11.632 14.440  35.657  1.00 8.41   ? 245 ARG B O   1 
ATOM   4291 C  CB  . ARG B 1 245 ? -9.942  16.766  34.665  1.00 8.75   ? 245 ARG B CB  1 
ATOM   4292 C  CG  . ARG B 1 245 ? -8.813  17.026  35.720  1.00 11.09  ? 245 ARG B CG  1 
ATOM   4293 C  CD  . ARG B 1 245 ? -8.943  18.430  36.298  1.00 12.04  ? 245 ARG B CD  1 
ATOM   4294 N  NE  . ARG B 1 245 ? -7.654  18.730  37.001  1.00 11.10  ? 245 ARG B NE  1 
ATOM   4295 C  CZ  . ARG B 1 245 ? -7.472  19.708  37.864  1.00 9.19   ? 245 ARG B CZ  1 
ATOM   4296 N  NH1 . ARG B 1 245 ? -8.445  20.513  38.246  1.00 8.37   ? 245 ARG B NH1 1 
ATOM   4297 N  NH2 . ARG B 1 245 ? -6.205  19.947  38.331  1.00 12.08  ? 245 ARG B NH2 1 
ATOM   4298 N  N   . PRO B 1 246 ? -9.581  13.636  35.960  1.00 7.18   ? 246 PRO B N   1 
ATOM   4299 C  CA  . PRO B 1 246 ? -10.016 12.830  37.094  1.00 7.55   ? 246 PRO B CA  1 
ATOM   4300 C  C   . PRO B 1 246 ? -10.347 13.675  38.328  1.00 6.97   ? 246 PRO B C   1 
ATOM   4301 O  O   . PRO B 1 246 ? -10.035 14.849  38.466  1.00 8.38   ? 246 PRO B O   1 
ATOM   4302 C  CB  . PRO B 1 246 ? -8.808  11.955  37.395  1.00 10.48  ? 246 PRO B CB  1 
ATOM   4303 C  CG  . PRO B 1 246 ? -7.885  12.151  36.204  1.00 16.21  ? 246 PRO B CG  1 
ATOM   4304 C  CD  . PRO B 1 246 ? -8.138  13.502  35.583  1.00 9.57   ? 246 PRO B CD  1 
ATOM   4305 N  N   . ALA B 1 247 ? -11.006 13.008  39.288  1.00 8.53   ? 247 ALA B N   1 
ATOM   4306 C  CA  . ALA B 1 247 ? -11.349 13.620  40.574  1.00 7.82   ? 247 ALA B CA  1 
ATOM   4307 C  C   . ALA B 1 247 ? -10.098 14.143  41.283  1.00 7.50   ? 247 ALA B C   1 
ATOM   4308 O  O   . ALA B 1 247 ? -9.065  13.500  41.329  1.00 8.94   ? 247 ALA B O   1 
ATOM   4309 C  CB  . ALA B 1 247 ? -12.074 12.628  41.440  1.00 9.99   ? 247 ALA B CB  1 
ATOM   4310 N  N   . GLN B 1 248 ? -10.260 15.343  41.864  1.00 7.62   ? 248 GLN B N   1 
ATOM   4311 C  CA  . GLN B 1 248 ? -9.225  16.047  42.605  1.00 8.74   ? 248 GLN B CA  1 
ATOM   4312 C  C   . GLN B 1 248 ? -9.546  16.031  44.089  1.00 8.44   ? 248 GLN B C   1 
ATOM   4313 O  O   . GLN B 1 248 ? -10.686 15.846  44.468  1.00 9.65   ? 248 GLN B O   1 
ATOM   4314 C  CB  . GLN B 1 248 ? -9.207  17.467  42.057  1.00 9.00   ? 248 GLN B CB  1 
ATOM   4315 C  CG  . GLN B 1 248 ? -8.868  17.579  40.569  1.00 8.91   ? 248 GLN B CG  1 
ATOM   4316 C  CD  . GLN B 1 248 ? -7.543  16.901  40.293  1.00 10.19  ? 248 GLN B CD  1 
ATOM   4317 O  OE1 . GLN B 1 248 ? -6.499  17.242  40.815  1.00 12.05  ? 248 GLN B OE1 1 
ATOM   4318 N  NE2 . GLN B 1 248 ? -7.516  16.020  39.321  1.00 10.16  ? 248 GLN B NE2 1 
ATOM   4319 N  N   . PRO B 1 249 ? -8.569  16.335  44.953  1.00 9.92   ? 249 PRO B N   1 
ATOM   4320 C  CA  . PRO B 1 249 ? -8.777  16.321  46.376  1.00 11.05  ? 249 PRO B CA  1 
ATOM   4321 C  C   . PRO B 1 249 ? -9.875  17.297  46.810  1.00 8.95   ? 249 PRO B C   1 
ATOM   4322 O  O   . PRO B 1 249 ? -9.820  18.493  46.434  1.00 9.30   ? 249 PRO B O   1 
ATOM   4323 C  CB  . PRO B 1 249 ? -7.411  16.681  46.999  1.00 14.36  ? 249 PRO B CB  1 
ATOM   4324 C  CG  . PRO B 1 249 ? -6.447  16.258  45.944  1.00 15.63  ? 249 PRO B CG  1 
ATOM   4325 C  CD  . PRO B 1 249 ? -7.157  16.554  44.618  1.00 14.28  ? 249 PRO B CD  1 
ATOM   4326 N  N   . LEU B 1 250 ? -10.731 16.810  47.698  1.00 10.53  ? 250 LEU B N   1 
ATOM   4327 C  CA  . LEU B 1 250 ? -11.810 17.657  48.203  1.00 9.69   ? 250 LEU B CA  1 
ATOM   4328 C  C   . LEU B 1 250 ? -11.287 18.761  49.114  1.00 10.15  ? 250 LEU B C   1 
ATOM   4329 O  O   . LEU B 1 250 ? -11.859 19.853  49.182  1.00 10.24  ? 250 LEU B O   1 
ATOM   4330 C  CB  . LEU B 1 250 ? -12.839 16.821  48.943  1.00 12.21  ? 250 LEU B CB  1 
ATOM   4331 C  CG  . LEU B 1 250 ? -14.156 17.478  49.324  1.00 13.45  ? 250 LEU B CG  1 
ATOM   4332 C  CD1 . LEU B 1 250 ? -14.841 18.050  48.077  1.00 12.58  ? 250 LEU B CD1 1 
ATOM   4333 C  CD2 . LEU B 1 250 ? -15.100 16.503  50.096  1.00 18.43  ? 250 LEU B CD2 1 
ATOM   4334 N  N   . LYS B 1 251 ? -10.187 18.497  49.831  1.00 11.78  ? 251 LYS B N   1 
ATOM   4335 C  CA  . LYS B 1 251 ? -9.596  19.453  50.775  1.00 12.85  ? 251 LYS B CA  1 
ATOM   4336 C  C   . LYS B 1 251 ? -10.644 19.954  51.759  1.00 12.99  ? 251 LYS B C   1 
ATOM   4337 O  O   . LYS B 1 251 ? -11.494 19.181  52.226  1.00 16.91  ? 251 LYS B O   1 
ATOM   4338 C  CB  . LYS B 1 251 ? -8.853  20.522  49.973  1.00 15.48  ? 251 LYS B CB  1 
ATOM   4339 C  CG  . LYS B 1 251 ? -7.729  19.928  49.137  1.00 20.17  ? 251 LYS B CG  1 
ATOM   4340 C  CD  . LYS B 1 251 ? -6.734  20.860  48.583  1.00 26.66  ? 251 LYS B CD  1 
ATOM   4341 C  CE  . LYS B 1 251 ? -5.502  20.091  48.154  1.00 28.88  ? 251 LYS B CE  1 
ATOM   4342 N  NZ  . LYS B 1 251 ? -4.571  20.978  47.409  1.00 30.39  ? 251 LYS B NZ  1 
ATOM   4343 N  N   . ASN B 1 252 ? -10.649 21.259  52.003  1.00 14.11  ? 252 ASN B N   1 
ATOM   4344 C  CA  . ASN B 1 252 ? -11.504 21.822  53.025  1.00 18.49  ? 252 ASN B CA  1 
ATOM   4345 C  C   . ASN B 1 252 ? -12.809 22.261  52.394  1.00 22.53  ? 252 ASN B C   1 
ATOM   4346 O  O   . ASN B 1 252 ? -13.017 23.513  52.373  1.00 23.60  ? 252 ASN B O   1 
ATOM   4347 C  CB  . ASN B 1 252 ? -10.777 22.996  53.761  1.00 20.71  ? 252 ASN B CB  1 
ATOM   4348 C  CG  . ASN B 1 252 ? -11.491 23.554  54.990  1.00 28.21  ? 252 ASN B CG  1 
ATOM   4349 O  OD1 . ASN B 1 252 ? -11.908 22.775  55.852  1.00 44.81  ? 252 ASN B OD1 1 
ATOM   4350 N  ND2 . ASN B 1 252 ? -11.680 24.887  55.084  1.00 26.91  ? 252 ASN B ND2 1 
ATOM   4351 N  N   . ARG B 1 253 ? -13.589 21.274  51.809  1.00 16.88  ? 253 ARG B N   1 
ATOM   4352 C  CA  . ARG B 1 253 ? -14.846 21.667  51.218  1.00 9.51   ? 253 ARG B CA  1 
ATOM   4353 C  C   . ARG B 1 253 ? -15.913 20.712  51.667  1.00 11.10  ? 253 ARG B C   1 
ATOM   4354 O  O   . ARG B 1 253 ? -15.657 19.552  51.952  1.00 18.30  ? 253 ARG B O   1 
ATOM   4355 C  CB  . ARG B 1 253 ? -14.730 21.602  49.702  1.00 9.74   ? 253 ARG B CB  1 
ATOM   4356 C  CG  . ARG B 1 253 ? -13.872 22.776  49.218  1.00 9.65   ? 253 ARG B CG  1 
ATOM   4357 C  CD  . ARG B 1 253 ? -13.725 22.776  47.716  1.00 9.16   ? 253 ARG B CD  1 
ATOM   4358 N  NE  . ARG B 1 253 ? -12.956 21.620  47.266  1.00 7.92   ? 253 ARG B NE  1 
ATOM   4359 C  CZ  . ARG B 1 253 ? -12.697 21.347  45.963  1.00 6.95   ? 253 ARG B CZ  1 
ATOM   4360 N  NH1 . ARG B 1 253 ? -13.296 22.027  44.969  1.00 7.83   ? 253 ARG B NH1 1 
ATOM   4361 N  NH2 . ARG B 1 253 ? -11.855 20.379  45.658  1.00 8.34   ? 253 ARG B NH2 1 
ATOM   4362 N  N   . GLN B 1 254 ? -17.154 21.220  51.663  1.00 11.31  ? 254 GLN B N   1 
ATOM   4363 C  CA  . GLN B 1 254 ? -18.360 20.451  51.934  1.00 12.85  ? 254 GLN B CA  1 
ATOM   4364 C  C   . GLN B 1 254 ? -19.196 20.427  50.671  1.00 9.97   ? 254 GLN B C   1 
ATOM   4365 O  O   . GLN B 1 254 ? -19.426 21.450  50.018  1.00 15.01  ? 254 GLN B O   1 
ATOM   4366 C  CB  . GLN B 1 254 ? -19.043 21.004  53.197  1.00 24.28  ? 254 GLN B CB  1 
ATOM   4367 C  CG  . GLN B 1 254 ? -18.311 20.699  54.527  1.00 30.54  ? 254 GLN B CG  1 
ATOM   4368 C  CD  . GLN B 1 254 ? -19.027 20.647  55.871  1.00 38.93  ? 254 GLN B CD  1 
ATOM   4369 O  OE1 . GLN B 1 254 ? -19.019 21.618  56.648  1.00 57.16  ? 254 GLN B OE1 1 
ATOM   4370 N  NE2 . GLN B 1 254 ? -19.518 19.462  56.231  1.00 47.67  ? 254 GLN B NE2 1 
ATOM   4371 N  N   . ILE B 1 255 ? -19.656 19.230  50.322  1.00 10.20  ? 255 ILE B N   1 
ATOM   4372 C  CA  . ILE B 1 255 ? -20.659 19.063  49.265  1.00 9.37   ? 255 ILE B CA  1 
ATOM   4373 C  C   . ILE B 1 255 ? -22.042 19.054  49.905  1.00 9.93   ? 255 ILE B C   1 
ATOM   4374 O  O   . ILE B 1 255 ? -22.242 18.291  50.855  1.00 12.83  ? 255 ILE B O   1 
ATOM   4375 C  CB  . ILE B 1 255 ? -20.374 17.809  48.438  1.00 9.77   ? 255 ILE B CB  1 
ATOM   4376 C  CG1 . ILE B 1 255 ? -18.931 17.824  47.872  1.00 9.92   ? 255 ILE B CG1 1 
ATOM   4377 C  CG2 . ILE B 1 255 ? -21.422 17.759  47.319  1.00 11.24  ? 255 ILE B CG2 1 
ATOM   4378 C  CD1 . ILE B 1 255 ? -18.559 16.592  47.110  1.00 11.13  ? 255 ILE B CD1 1 
ATOM   4379 N  N   . LYS B 1 256 ? -22.944 19.915  49.422  1.00 8.09   ? 256 LYS B N   1 
ATOM   4380 C  CA  . LYS B 1 256 ? -24.292 20.014  49.976  1.00 9.20   ? 256 LYS B CA  1 
ATOM   4381 C  C   . LYS B 1 256 ? -25.270 19.370  48.999  1.00 9.85   ? 256 LYS B C   1 
ATOM   4382 O  O   . LYS B 1 256 ? -25.093 19.487  47.799  1.00 11.22  ? 256 LYS B O   1 
ATOM   4383 C  CB  . LYS B 1 256 ? -24.589 21.477  50.260  1.00 11.80  ? 256 LYS B CB  1 
ATOM   4384 C  CG  . LYS B 1 256 ? -23.677 22.101  51.334  1.00 17.23  ? 256 LYS B CG  1 
ATOM   4385 C  CD  . LYS B 1 256 ? -23.913 23.556  51.642  1.00 22.95  ? 256 LYS B CD  1 
ATOM   4386 C  CE  . LYS B 1 256 ? -22.743 24.120  52.446  1.00 33.38  ? 256 LYS B CE  1 
ATOM   4387 N  NZ  . LYS B 1 256 ? -23.005 25.545  52.767  1.00 42.25  ? 256 LYS B NZ  1 
ATOM   4388 N  N   . ALA B 1 257 ? -26.271 18.709  49.544  1.00 9.87   ? 257 ALA B N   1 
ATOM   4389 C  CA  . ALA B 1 257 ? -27.368 18.108  48.761  1.00 10.72  ? 257 ALA B CA  1 
ATOM   4390 C  C   . ALA B 1 257 ? -28.605 18.957  48.900  1.00 10.70  ? 257 ALA B C   1 
ATOM   4391 O  O   . ALA B 1 257 ? -28.984 19.366  50.041  1.00 12.15  ? 257 ALA B O   1 
ATOM   4392 C  CB  . ALA B 1 257 ? -27.681 16.676  49.158  1.00 12.38  ? 257 ALA B CB  1 
ATOM   4393 N  N   . SER B 1 258 ? -29.332 19.162  47.811  1.00 10.26  ? 258 SER B N   1 
ATOM   4394 C  CA  . SER B 1 258 ? -30.636 19.819  47.793  1.00 10.71  ? 258 SER B CA  1 
ATOM   4395 C  C   . SER B 1 258 ? -31.832 18.971  48.229  1.00 11.87  ? 258 SER B C   1 
ATOM   4396 O  O   . SER B 1 258 ? -32.933 19.507  48.313  1.00 19.06  ? 258 SER B O   1 
ATOM   4397 C  CB  . SER B 1 258 ? -30.935 20.363  46.450  1.00 10.89  ? 258 SER B CB  1 
ATOM   4398 O  OG  . SER B 1 258 ? -31.307 19.390  45.516  1.00 11.35  ? 258 SER B OG  1 
ATOM   4399 N  N   . PHE B 1 259 ? -31.545 17.715  48.501  1.00 13.93  ? 259 PHE B N   1 
ATOM   4400 C  CA  . PHE B 1 259 ? -32.622 16.733  48.614  1.00 17.26  ? 259 PHE B CA  1 
ATOM   4401 C  C   . PHE B 1 259 ? -32.283 15.785  49.759  1.00 23.56  ? 259 PHE B C   1 
ATOM   4402 O  O   . PHE B 1 259 ? -31.059 15.651  50.063  1.00 20.43  ? 259 PHE B O   1 
ATOM   4403 C  CB  . PHE B 1 259 ? -32.770 15.927  47.294  1.00 16.90  ? 259 PHE B CB  1 
ATOM   4404 C  CG  . PHE B 1 259 ? -31.480 15.195  46.917  1.00 15.48  ? 259 PHE B CG  1 
ATOM   4405 C  CD1 . PHE B 1 259 ? -30.482 15.898  46.267  1.00 13.84  ? 259 PHE B CD1 1 
ATOM   4406 C  CD2 . PHE B 1 259 ? -31.199 13.854  47.294  1.00 18.46  ? 259 PHE B CD2 1 
ATOM   4407 C  CE1 . PHE B 1 259 ? -29.267 15.307  45.997  1.00 17.16  ? 259 PHE B CE1 1 
ATOM   4408 C  CE2 . PHE B 1 259 ? -29.924 13.307  47.017  1.00 21.43  ? 259 PHE B CE2 1 
ATOM   4409 C  CZ  . PHE B 1 259 ? -28.954 14.046  46.415  1.00 19.34  ? 259 PHE B CZ  1 
ATOM   4410 N  N   . LYS B 1 260 ? -33.335 15.170  50.268  1.00 33.65  ? 260 LYS B N   1 
ATOM   4411 C  CA  . LYS B 1 260 ? -33.496 14.045  51.198  1.00 43.76  ? 260 LYS B CA  1 
ATOM   4412 C  C   . LYS B 1 260 ? -33.617 14.445  52.673  1.00 44.76  ? 260 LYS B C   1 
ATOM   4413 O  O   . LYS B 1 260 ? -32.649 14.878  53.318  1.00 70.98  ? 260 LYS B O   1 
ATOM   4414 C  CB  . LYS B 1 260 ? -32.710 12.766  50.869  1.00 38.84  ? 260 LYS B CB  1 
ATOM   4415 C  CG  . LYS B 1 260 ? -33.253 12.024  49.652  1.00 36.07  ? 260 LYS B CG  1 
ATOM   4416 C  CD  . LYS B 1 260 ? -34.749 12.219  49.442  1.00 48.72  ? 260 LYS B CD  1 
ATOM   4417 C  CE  . LYS B 1 260 ? -35.002 13.378  48.476  1.00 40.99  ? 260 LYS B CE  1 
ATOM   4418 N  NZ  . LYS B 1 260 ? -35.431 12.885  47.122  1.00 70.42  ? 260 LYS B NZ  1 
ATOM   4419 O  OXT . LYS B 1 260 ? -34.731 14.326  53.202  1.00 57.41  ? 260 LYS B OXT 1 
HETATM 4420 ZN ZN  . ZN  C 2 .   ? -3.540  0.039   0.553   1.00 5.77   ? 301 ZN  A ZN  1 
HETATM 4421 CL CL  . 7VZ D 3 .   ? -5.960  3.852   5.884   1.00 35.09  ? 302 7VZ A CL  1 
HETATM 4422 C  C10 . 7VZ D 3 .   ? -5.908  3.456   4.244   1.00 15.28  ? 302 7VZ A C10 1 
HETATM 4423 C  C11 . 7VZ D 3 .   ? -6.051  2.180   3.728   1.00 10.15  ? 302 7VZ A C11 1 
HETATM 4424 C  C14 . 7VZ D 3 .   ? -6.383  1.028   4.542   1.00 9.83   ? 302 7VZ A C14 1 
HETATM 4425 O  O16 . 7VZ D 3 .   ? -6.661  -0.065  3.871   1.00 9.03   ? 302 7VZ A O16 1 
HETATM 4426 C  C17 . 7VZ D 3 .   ? -7.155  -1.270  4.540   1.00 10.08  ? 302 7VZ A C17 1 
HETATM 4427 O  O15 . 7VZ D 3 .   ? -6.390  0.991   5.771   1.00 14.94  ? 302 7VZ A O15 1 
HETATM 4428 C  C9  . 7VZ D 3 .   ? -5.389  4.497   3.443   1.00 15.25  ? 302 7VZ A C9  1 
HETATM 4429 C  C8  . 7VZ D 3 .   ? -5.248  4.304   2.058   1.00 12.69  ? 302 7VZ A C8  1 
HETATM 4430 C  C7  . 7VZ D 3 .   ? -5.424  3.032   1.495   1.00 8.35   ? 302 7VZ A C7  1 
HETATM 4431 S  S4  . 7VZ D 3 .   ? -4.963  2.724   -0.140  1.00 7.44   ? 302 7VZ A S4  1 
HETATM 4432 O  O6  . 7VZ D 3 .   ? -3.670  3.300   -0.298  1.00 7.95   ? 302 7VZ A O6  1 
HETATM 4433 N  N1  . 7VZ D 3 .   ? -4.925  1.193   -0.371  1.00 6.80   ? 302 7VZ A N1  1 
HETATM 4434 O  O5  . 7VZ D 3 .   ? -5.967  3.218   -0.977  1.00 9.64   ? 302 7VZ A O5  1 
HETATM 4435 C  C12 . 7VZ D 3 .   ? -5.806  2.028   2.345   1.00 8.24   ? 302 7VZ A C12 1 
HETATM 4436 S  S21 . 7VZ D 3 .   ? -4.707  5.724   1.044   1.00 14.24  ? 302 7VZ A S21 1 
HETATM 4437 C  C22 . 7VZ D 3 .   ? -5.124  7.184   2.000   1.00 13.96  ? 302 7VZ A C22 1 
HETATM 4438 C  C23 . 7VZ D 3 .   ? -3.951  7.458   2.915   1.00 15.34  ? 302 7VZ A C23 1 
HETATM 4439 C  C24 . 7VZ D 3 .   ? -4.163  8.720   3.749   1.00 16.77  ? 302 7VZ A C24 1 
HETATM 4440 C  C25 . 7VZ D 3 .   ? -4.231  9.911   2.747   1.00 19.30  ? 302 7VZ A C25 1 
HETATM 4441 C  C26 . 7VZ D 3 .   ? -5.417  9.757   1.765   1.00 15.99  ? 302 7VZ A C26 1 
HETATM 4442 C  C27 . 7VZ D 3 .   ? -5.383  8.363   1.054   1.00 17.37  ? 302 7VZ A C27 1 
HETATM 4443 C  C   . ACT E 4 .   ? -0.263  6.117   -18.212 1.00 31.73  ? 303 ACT A C   1 
HETATM 4444 O  O   . ACT E 4 .   ? -0.886  5.170   -18.894 1.00 20.37  ? 303 ACT A O   1 
HETATM 4445 O  OXT . ACT E 4 .   ? 0.971   6.369   -18.339 1.00 54.87  ? 303 ACT A OXT 1 
HETATM 4446 C  CH3 . ACT E 4 .   ? -1.029  7.005   -17.188 1.00 14.12  ? 303 ACT A CH3 1 
HETATM 4447 S  S   . DMS F 5 .   ? -11.559 -9.905  0.846   1.00 16.78  ? 304 DMS A S   1 
HETATM 4448 O  O   . DMS F 5 .   ? -12.170 -11.267 1.270   1.00 22.77  ? 304 DMS A O   1 
HETATM 4449 C  C1  . DMS F 5 .   ? -12.712 -8.666  1.330   1.00 19.97  ? 304 DMS A C1  1 
HETATM 4450 C  C2  . DMS F 5 .   ? -11.819 -9.784  -0.888  1.00 16.39  ? 304 DMS A C2  1 
HETATM 4451 ZN ZN  . ZN  G 2 .   ? -16.534 20.720  31.223  1.00 6.80   ? 301 ZN  B ZN  1 
HETATM 4452 CL CL  . 7VZ H 3 .   ? -13.956 24.552  25.916  1.00 43.12  ? 302 7VZ B CL  1 
HETATM 4453 C  C10 . 7VZ H 3 .   ? -14.164 24.130  27.551  1.00 16.74  ? 302 7VZ B C10 1 
HETATM 4454 C  C11 . 7VZ H 3 .   ? -13.998 22.830  28.077  1.00 11.38  ? 302 7VZ B C11 1 
HETATM 4455 C  C14 . 7VZ H 3 .   ? -13.710 21.702  27.265  1.00 9.84   ? 302 7VZ B C14 1 
HETATM 4456 O  O16 . 7VZ H 3 .   ? -13.429 20.634  27.920  1.00 9.46   ? 302 7VZ B O16 1 
HETATM 4457 C  C17 . 7VZ H 3 .   ? -13.022 19.383  27.222  1.00 11.15  ? 302 7VZ B C17 1 
HETATM 4458 O  O15 . 7VZ H 3 .   ? -13.716 21.682  25.973  1.00 15.98  ? 302 7VZ B O15 1 
HETATM 4459 C  C9  . 7VZ H 3 .   ? -14.582 25.174  28.366  1.00 16.47  ? 302 7VZ B C9  1 
HETATM 4460 C  C8  . 7VZ H 3 .   ? -14.850 24.990  29.731  1.00 13.90  ? 302 7VZ B C8  1 
HETATM 4461 C  C7  . 7VZ H 3 .   ? -14.684 23.680  30.278  1.00 9.45   ? 302 7VZ B C7  1 
HETATM 4462 S  S4  . 7VZ H 3 .   ? -15.135 23.397  31.887  1.00 8.51   ? 302 7VZ B S4  1 
HETATM 4463 O  O6  . 7VZ H 3 .   ? -14.098 23.962  32.747  1.00 10.19  ? 302 7VZ B O6  1 
HETATM 4464 N  N1  . 7VZ H 3 .   ? -15.268 21.712  31.982  1.00 7.89   ? 302 7VZ B N1  1 
HETATM 4465 O  O5  . 7VZ H 3 .   ? -16.427 23.979  32.071  1.00 8.52   ? 302 7VZ B O5  1 
HETATM 4466 C  C12 . 7VZ H 3 .   ? -14.252 22.654  29.454  1.00 8.62   ? 302 7VZ B C12 1 
HETATM 4467 S  S21 . 7VZ H 3 .   ? -15.383 26.410  30.720  1.00 14.38  ? 302 7VZ B S21 1 
HETATM 4468 C  C22 . 7VZ H 3 .   ? -14.922 27.855  29.743  1.00 13.29  ? 302 7VZ B C22 1 
HETATM 4469 C  C23 . 7VZ H 3 .   ? -16.141 28.146  28.893  1.00 15.18  ? 302 7VZ B C23 1 
HETATM 4470 C  C24 . 7VZ H 3 .   ? -15.946 29.424  28.074  1.00 19.21  ? 302 7VZ B C24 1 
HETATM 4471 C  C25 . 7VZ H 3 .   ? -15.875 30.537  29.097  1.00 20.13  ? 302 7VZ B C25 1 
HETATM 4472 C  C26 . 7VZ H 3 .   ? -14.558 30.343  29.895  1.00 17.48  ? 302 7VZ B C26 1 
HETATM 4473 C  C27 . 7VZ H 3 .   ? -14.593 29.002  30.693  1.00 17.50  ? 302 7VZ B C27 1 
HETATM 4474 S  S   . DMS I 5 .   ? -8.476  10.779  30.918  1.00 15.86  ? 303 DMS B S   1 
HETATM 4475 O  O   . DMS I 5 .   ? -7.944  9.415   30.467  1.00 23.65  ? 303 DMS B O   1 
HETATM 4476 C  C1  . DMS I 5 .   ? -7.320  11.987  30.433  1.00 29.87  ? 303 DMS B C1  1 
HETATM 4477 C  C2  . DMS I 5 .   ? -8.189  10.913  32.647  1.00 15.90  ? 303 DMS B C2  1 
HETATM 4478 O  O   . HOH J 6 .   ? -10.834 -2.056  28.575  1.00 47.09  ? 401 HOH A O   1 
HETATM 4479 O  O   . HOH J 6 .   ? 15.227  -3.637  2.624   1.00 173.32 ? 402 HOH A O   1 
HETATM 4480 O  O   . HOH J 6 .   ? -21.836 -5.101  -6.266  1.00 33.71  ? 403 HOH A O   1 
HETATM 4481 O  O   . HOH J 6 .   ? -14.438 -7.421  21.690  1.00 34.67  ? 404 HOH A O   1 
HETATM 4482 O  O   . HOH J 6 .   ? 19.991  -7.806  -6.122  1.00 33.33  ? 405 HOH A O   1 
HETATM 4483 O  O   . HOH J 6 .   ? 2.112   12.462  10.060  1.00 32.46  ? 406 HOH A O   1 
HETATM 4484 O  O   . HOH J 6 .   ? 0.929   -13.203 -18.316 1.00 21.80  ? 407 HOH A O   1 
HETATM 4485 O  O   . HOH J 6 .   ? 2.741   0.859   21.667  1.00 35.58  ? 408 HOH A O   1 
HETATM 4486 O  O   . HOH J 6 .   ? -16.492 1.481   17.064  1.00 29.47  ? 409 HOH A O   1 
HETATM 4487 O  O   . HOH J 6 .   ? 3.652   -7.205  21.092  1.00 25.51  ? 410 HOH A O   1 
HETATM 4488 O  O   . HOH J 6 .   ? 3.816   -3.611  22.557  1.00 29.19  ? 411 HOH A O   1 
HETATM 4489 O  O   . HOH J 6 .   ? -0.078  17.644  -13.777 1.00 27.37  ? 412 HOH A O   1 
HETATM 4490 O  O   . HOH J 6 .   ? 8.431   -10.511 19.487  1.00 30.79  ? 413 HOH A O   1 
HETATM 4491 O  O   . HOH J 6 .   ? 0.380   23.561  -4.201  1.00 22.34  ? 414 HOH A O   1 
HETATM 4492 O  O   . HOH J 6 .   ? -18.096 -6.720  16.005  1.00 40.63  ? 415 HOH A O   1 
HETATM 4493 O  O   . HOH J 6 .   ? 9.687   -2.191  -25.336 1.00 36.88  ? 416 HOH A O   1 
HETATM 4494 O  O   . HOH J 6 .   ? 6.661   16.451  -17.488 1.00 27.70  ? 417 HOH A O   1 
HETATM 4495 O  O   . HOH J 6 .   ? 8.602   19.480  -2.845  1.00 27.70  ? 418 HOH A O   1 
HETATM 4496 O  O   . HOH J 6 .   ? -14.564 -0.592  -13.149 1.00 22.77  ? 419 HOH A O   1 
HETATM 4497 O  O   . HOH J 6 .   ? -0.306  3.347   -23.260 1.00 28.69  ? 420 HOH A O   1 
HETATM 4498 O  O   . HOH J 6 .   ? 2.314   14.357  -13.240 1.00 31.10  ? 421 HOH A O   1 
HETATM 4499 O  O   . HOH J 6 .   ? 10.638  -5.117  18.194  1.00 28.35  ? 422 HOH A O   1 
HETATM 4500 O  O   . HOH J 6 .   ? -17.022 -1.603  -14.127 1.00 31.85  ? 423 HOH A O   1 
HETATM 4501 O  O   . HOH J 6 .   ? -14.918 -2.017  12.897  1.00 29.88  ? 424 HOH A O   1 
HETATM 4502 O  O   . HOH J 6 .   ? 6.537   20.433  -6.094  1.00 34.78  ? 425 HOH A O   1 
HETATM 4503 O  O   . HOH J 6 .   ? 10.218  10.355  -14.176 1.00 26.36  ? 426 HOH A O   1 
HETATM 4504 O  O   . HOH J 6 .   ? -9.911  2.997   -18.617 1.00 34.00  ? 427 HOH A O   1 
HETATM 4505 O  O   . HOH J 6 .   ? 14.573  -18.937 6.598   1.00 40.01  ? 428 HOH A O   1 
HETATM 4506 O  O   . HOH J 6 .   ? -13.703 -12.141 3.209   1.00 33.24  ? 429 HOH A O   1 
HETATM 4507 O  O   . HOH J 6 .   ? -4.211  -9.719  -20.686 1.00 36.23  ? 430 HOH A O   1 
HETATM 4508 O  O   . HOH J 6 .   ? 5.036   4.423   -22.798 1.00 34.17  ? 431 HOH A O   1 
HETATM 4509 O  O   . HOH J 6 .   ? 15.261  -0.966  -17.497 1.00 46.25  ? 432 HOH A O   1 
HETATM 4510 O  O   . HOH J 6 .   ? -14.454 -1.522  -10.714 1.00 20.18  ? 433 HOH A O   1 
HETATM 4511 O  O   . HOH J 6 .   ? 9.163   19.020  9.913   1.00 34.90  ? 434 HOH A O   1 
HETATM 4512 O  O   . HOH J 6 .   ? -23.201 -3.901  -8.619  1.00 28.37  ? 435 HOH A O   1 
HETATM 4513 O  O   . HOH J 6 .   ? 13.814  -1.123  -13.189 1.00 29.84  ? 436 HOH A O   1 
HETATM 4514 O  O   . HOH J 6 .   ? 11.118  21.367  -1.782  1.00 46.56  ? 437 HOH A O   1 
HETATM 4515 O  O   . HOH J 6 .   ? -1.040  7.888   -13.091 1.00 17.76  ? 438 HOH A O   1 
HETATM 4516 O  O   . HOH J 6 .   ? 0.443   10.556  -9.531  1.00 9.02   ? 439 HOH A O   1 
HETATM 4517 O  O   . HOH J 6 .   ? -3.087  -12.985 -15.877 1.00 18.35  ? 440 HOH A O   1 
HETATM 4518 O  O   . HOH J 6 .   ? -12.799 -2.618  8.246   1.00 22.63  ? 441 HOH A O   1 
HETATM 4519 O  O   . HOH J 6 .   ? 6.343   -13.577 -17.100 1.00 32.78  ? 442 HOH A O   1 
HETATM 4520 O  O   . HOH J 6 .   ? -11.377 -7.471  21.278  1.00 30.54  ? 443 HOH A O   1 
HETATM 4521 O  O   . HOH J 6 .   ? -9.089  11.086  -12.131 1.00 18.35  ? 444 HOH A O   1 
HETATM 4522 O  O   . HOH J 6 .   ? -11.299 16.484  -8.671  1.00 33.78  ? 445 HOH A O   1 
HETATM 4523 O  O   . HOH J 6 .   ? 5.433   10.711  18.021  1.00 32.34  ? 446 HOH A O   1 
HETATM 4524 O  O   . HOH J 6 .   ? -11.277 -9.867  -9.296  1.00 22.46  ? 447 HOH A O   1 
HETATM 4525 O  O   . HOH J 6 .   ? -23.626 1.997   -8.671  1.00 26.09  ? 448 HOH A O   1 
HETATM 4526 O  O   . HOH J 6 .   ? 7.678   -20.380 9.779   1.00 16.87  ? 449 HOH A O   1 
HETATM 4527 O  O   . HOH J 6 .   ? 3.353   -20.852 4.306   1.00 41.27  ? 450 HOH A O   1 
HETATM 4528 O  O   . HOH J 6 .   ? -19.885 -6.343  12.454  1.00 37.80  ? 451 HOH A O   1 
HETATM 4529 O  O   . HOH J 6 .   ? -8.920  -2.227  0.135   1.00 8.01   ? 452 HOH A O   1 
HETATM 4530 O  O   . HOH J 6 .   ? 10.011  12.789  -10.556 1.00 18.31  ? 453 HOH A O   1 
HETATM 4531 O  O   . HOH J 6 .   ? -4.061  -3.016  22.379  1.00 32.25  ? 454 HOH A O   1 
HETATM 4532 O  O   . HOH J 6 .   ? -5.484  -10.110 -16.314 1.00 18.76  ? 455 HOH A O   1 
HETATM 4533 O  O   . HOH J 6 .   ? 8.384   -18.783 0.759   1.00 42.23  ? 456 HOH A O   1 
HETATM 4534 O  O   . HOH J 6 .   ? -11.656 10.023  -12.555 1.00 22.22  ? 457 HOH A O   1 
HETATM 4535 O  O   . HOH J 6 .   ? 7.705   12.319  4.591   1.00 22.96  ? 458 HOH A O   1 
HETATM 4536 O  O   . HOH J 6 .   ? 3.909   -19.427 12.642  1.00 36.75  ? 459 HOH A O   1 
HETATM 4537 O  O   . HOH J 6 .   ? -10.202 -12.398 -15.373 1.00 38.01  ? 460 HOH A O   1 
HETATM 4538 O  O   . HOH J 6 .   ? 12.773  -4.191  13.074  1.00 24.82  ? 461 HOH A O   1 
HETATM 4539 O  O   . HOH J 6 .   ? -12.042 -13.905 6.499   1.00 19.37  ? 462 HOH A O   1 
HETATM 4540 O  O   . HOH J 6 .   ? 16.003  4.902   0.166   1.00 31.61  ? 463 HOH A O   1 
HETATM 4541 O  O   . HOH J 6 .   ? -7.640  -6.824  -13.311 1.00 10.26  ? 464 HOH A O   1 
HETATM 4542 O  O   . HOH J 6 .   ? 0.244   -16.472 -1.473  1.00 12.83  ? 465 HOH A O   1 
HETATM 4543 O  O   . HOH J 6 .   ? 11.461  7.477   11.250  1.00 27.02  ? 466 HOH A O   1 
HETATM 4544 O  O   . HOH J 6 .   ? 4.241   -14.713 -13.217 1.00 18.56  ? 467 HOH A O   1 
HETATM 4545 O  O   . HOH J 6 .   ? 6.820   -6.584  -4.508  1.00 8.27   ? 468 HOH A O   1 
HETATM 4546 O  O   . HOH J 6 .   ? -13.768 6.889   -14.065 1.00 16.80  ? 469 HOH A O   1 
HETATM 4547 O  O   . HOH J 6 .   ? 12.600  -13.006 -0.439  1.00 33.31  ? 470 HOH A O   1 
HETATM 4548 O  O   . HOH J 6 .   ? 3.602   12.297  -11.848 1.00 15.11  ? 471 HOH A O   1 
HETATM 4549 O  O   . HOH J 6 .   ? -5.658  -11.687 -2.285  1.00 7.44   ? 472 HOH A O   1 
HETATM 4550 O  O   . HOH J 6 .   ? 13.148  -1.242  8.977   1.00 23.86  ? 473 HOH A O   1 
HETATM 4551 O  O   . HOH J 6 .   ? -2.262  -13.791 4.340   1.00 8.40   ? 474 HOH A O   1 
HETATM 4552 O  O   . HOH J 6 .   ? -9.617  12.533  -7.846  1.00 17.71  ? 475 HOH A O   1 
HETATM 4553 O  O   . HOH J 6 .   ? -5.365  -14.201 14.979  1.00 29.81  ? 476 HOH A O   1 
HETATM 4554 O  O   . HOH J 6 .   ? 0.818   -18.046 8.267   1.00 26.41  ? 477 HOH A O   1 
HETATM 4555 O  O   . HOH J 6 .   ? 11.602  -12.373 -2.838  1.00 33.12  ? 478 HOH A O   1 
HETATM 4556 O  O   . HOH J 6 .   ? -6.066  -11.307 18.927  1.00 21.38  ? 479 HOH A O   1 
HETATM 4557 O  O   . HOH J 6 .   ? 14.695  -5.981  6.811   1.00 19.34  ? 480 HOH A O   1 
HETATM 4558 O  O   . HOH J 6 .   ? 15.378  -13.680 7.975   1.00 32.13  ? 481 HOH A O   1 
HETATM 4559 O  O   . HOH J 6 .   ? 11.385  -5.288  -7.688  1.00 16.93  ? 482 HOH A O   1 
HETATM 4560 O  O   . HOH J 6 .   ? 15.606  8.289   -11.193 1.00 28.65  ? 483 HOH A O   1 
HETATM 4561 O  O   . HOH J 6 .   ? 13.121  -9.390  -1.350  1.00 26.55  ? 484 HOH A O   1 
HETATM 4562 O  O   . HOH J 6 .   ? 13.177  1.961   -18.713 1.00 35.24  ? 485 HOH A O   1 
HETATM 4563 O  O   . HOH J 6 .   ? -6.380  -14.013 -8.630  1.00 10.87  ? 486 HOH A O   1 
HETATM 4564 O  O   . HOH J 6 .   ? -9.060  19.741  -0.517  1.00 45.33  ? 487 HOH A O   1 
HETATM 4565 O  O   . HOH J 6 .   ? -1.738  2.311   22.433  1.00 35.07  ? 488 HOH A O   1 
HETATM 4566 O  O   . HOH J 6 .   ? -12.741 -11.701 10.712  1.00 22.01  ? 489 HOH A O   1 
HETATM 4567 O  O   . HOH J 6 .   ? 3.782   16.300  -11.164 1.00 29.73  ? 490 HOH A O   1 
HETATM 4568 O  O   . HOH J 6 .   ? 8.484   -2.028  18.495  1.00 22.03  ? 491 HOH A O   1 
HETATM 4569 O  O   . HOH J 6 .   ? 11.952  -16.695 2.321   1.00 22.09  ? 492 HOH A O   1 
HETATM 4570 O  O   . HOH J 6 .   ? 13.175  1.501   -16.218 1.00 39.80  ? 493 HOH A O   1 
HETATM 4571 O  O   . HOH J 6 .   ? -15.410 8.967   -4.766  1.00 15.77  ? 494 HOH A O   1 
HETATM 4572 O  O   . HOH J 6 .   ? -7.826  -17.260 -5.765  1.00 33.21  ? 495 HOH A O   1 
HETATM 4573 O  O   . HOH J 6 .   ? -2.495  9.110   6.657   1.00 23.18  ? 496 HOH A O   1 
HETATM 4574 O  O   . HOH J 6 .   ? -18.182 -4.393  15.054  1.00 37.81  ? 497 HOH A O   1 
HETATM 4575 O  O   . HOH J 6 .   ? 5.870   17.846  -7.603  1.00 18.53  ? 498 HOH A O   1 
HETATM 4576 O  O   . HOH J 6 .   ? -13.603 4.373   7.775   1.00 31.94  ? 499 HOH A O   1 
HETATM 4577 O  O   . HOH J 6 .   ? -6.707  -9.318  -5.086  1.00 8.52   ? 500 HOH A O   1 
HETATM 4578 O  O   . HOH J 6 .   ? -3.552  22.982  -3.849  1.00 11.86  ? 501 HOH A O   1 
HETATM 4579 O  O   . HOH J 6 .   ? -11.007 13.004  -4.323  1.00 27.86  ? 502 HOH A O   1 
HETATM 4580 O  O   . HOH J 6 .   ? -18.753 -1.979  -5.206  1.00 16.47  ? 503 HOH A O   1 
HETATM 4581 O  O   . HOH J 6 .   ? -10.080 15.728  -0.675  1.00 20.88  ? 504 HOH A O   1 
HETATM 4582 O  O   . HOH J 6 .   ? -15.994 2.444   7.623   1.00 33.03  ? 505 HOH A O   1 
HETATM 4583 O  O   . HOH J 6 .   ? -7.560  5.949   7.638   1.00 41.69  ? 506 HOH A O   1 
HETATM 4584 O  O   . HOH J 6 .   ? 2.759   -20.450 7.138   1.00 25.78  ? 507 HOH A O   1 
HETATM 4585 O  O   . HOH J 6 .   ? -0.914  15.232  5.724   1.00 24.52  ? 508 HOH A O   1 
HETATM 4586 O  O   . HOH J 6 .   ? 5.624   -8.679  20.637  1.00 36.31  ? 509 HOH A O   1 
HETATM 4587 O  O   . HOH J 6 .   ? -12.696 -9.705  6.332   1.00 20.32  ? 510 HOH A O   1 
HETATM 4588 O  O   . HOH J 6 .   ? 16.008  4.598   -5.125  1.00 23.76  ? 511 HOH A O   1 
HETATM 4589 O  O   . HOH J 6 .   ? -2.795  -6.782  -16.776 1.00 15.10  ? 512 HOH A O   1 
HETATM 4590 O  O   . HOH J 6 .   ? 8.310   4.112   -24.675 1.00 45.91  ? 513 HOH A O   1 
HETATM 4591 O  O   . HOH J 6 .   ? -21.771 1.620   -0.210  1.00 26.26  ? 514 HOH A O   1 
HETATM 4592 O  O   . HOH J 6 .   ? -19.456 9.328   -2.975  1.00 39.86  ? 515 HOH A O   1 
HETATM 4593 O  O   . HOH J 6 .   ? -25.437 -0.678  1.366   1.00 22.03  ? 516 HOH A O   1 
HETATM 4594 O  O   . HOH J 6 .   ? -13.057 -13.127 14.028  1.00 46.03  ? 517 HOH A O   1 
HETATM 4595 O  O   . HOH J 6 .   ? -5.916  -6.581  -15.343 1.00 18.60  ? 518 HOH A O   1 
HETATM 4596 O  O   . HOH J 6 .   ? 7.630   -18.823 7.840   1.00 13.56  ? 519 HOH A O   1 
HETATM 4597 O  O   . HOH J 6 .   ? -4.822  10.691  8.962   1.00 22.26  ? 520 HOH A O   1 
HETATM 4598 O  O   . HOH J 6 .   ? 7.286   -14.501 -6.089  1.00 21.43  ? 521 HOH A O   1 
HETATM 4599 O  O   . HOH J 6 .   ? 10.987  -17.847 9.002   1.00 25.80  ? 522 HOH A O   1 
HETATM 4600 O  O   . HOH J 6 .   ? -11.623 -4.395  -18.536 1.00 24.35  ? 523 HOH A O   1 
HETATM 4601 O  O   . HOH J 6 .   ? 13.285  -11.550 4.437   1.00 17.79  ? 524 HOH A O   1 
HETATM 4602 O  O   . HOH J 6 .   ? -2.049  -17.318 -14.856 1.00 31.20  ? 525 HOH A O   1 
HETATM 4603 O  O   . HOH J 6 .   ? -6.824  -11.359 -9.405  1.00 9.86   ? 526 HOH A O   1 
HETATM 4604 O  O   . HOH J 6 .   ? 13.672  -16.217 9.262   1.00 43.35  ? 527 HOH A O   1 
HETATM 4605 O  O   . HOH J 6 .   ? -15.074 -3.055  -5.125  1.00 15.40  ? 528 HOH A O   1 
HETATM 4606 O  O   . HOH J 6 .   ? 1.362   18.081  6.967   1.00 45.74  ? 529 HOH A O   1 
HETATM 4607 O  O   . HOH J 6 .   ? -5.264  17.898  3.462   1.00 24.42  ? 530 HOH A O   1 
HETATM 4608 O  O   . HOH J 6 .   ? 5.248   5.280   -19.285 1.00 40.80  ? 531 HOH A O   1 
HETATM 4609 O  O   . HOH J 6 .   ? 16.018  -5.692  -14.552 1.00 28.79  ? 532 HOH A O   1 
HETATM 4610 O  O   . HOH J 6 .   ? -21.408 3.009   -10.124 1.00 28.18  ? 533 HOH A O   1 
HETATM 4611 O  O   . HOH J 6 .   ? 3.192   -16.757 1.059   1.00 18.58  ? 534 HOH A O   1 
HETATM 4612 O  O   . HOH J 6 .   ? -23.221 -2.092  2.410   1.00 26.94  ? 535 HOH A O   1 
HETATM 4613 O  O   . HOH J 6 .   ? -15.238 -5.599  -6.577  1.00 27.71  ? 536 HOH A O   1 
HETATM 4614 O  O   . HOH J 6 .   ? 2.696   -7.237  19.107  1.00 26.81  ? 537 HOH A O   1 
HETATM 4615 O  O   . HOH J 6 .   ? -11.614 10.562  -8.192  1.00 11.60  ? 538 HOH A O   1 
HETATM 4616 O  O   . HOH J 6 .   ? 3.146   21.837  1.007   1.00 25.37  ? 539 HOH A O   1 
HETATM 4617 O  O   . HOH J 6 .   ? 10.378  20.931  2.164   1.00 25.18  ? 540 HOH A O   1 
HETATM 4618 O  O   . HOH J 6 .   ? 2.870   -15.029 -10.914 1.00 14.99  ? 541 HOH A O   1 
HETATM 4619 O  O   . HOH J 6 .   ? 15.313  11.447  2.519   1.00 40.69  ? 542 HOH A O   1 
HETATM 4620 O  O   . HOH J 6 .   ? 9.166   11.830  7.010   1.00 19.48  ? 543 HOH A O   1 
HETATM 4621 O  O   . HOH J 6 .   ? 14.565  6.471   7.408   1.00 36.21  ? 544 HOH A O   1 
HETATM 4622 O  O   . HOH J 6 .   ? 2.508   -16.596 -16.341 1.00 21.76  ? 545 HOH A O   1 
HETATM 4623 O  O   . HOH J 6 .   ? 0.987   3.092   -17.667 1.00 21.57  ? 546 HOH A O   1 
HETATM 4624 O  O   . HOH J 6 .   ? 5.849   -10.531 -8.628  1.00 13.20  ? 547 HOH A O   1 
HETATM 4625 O  O   . HOH J 6 .   ? -3.119  3.425   -19.322 1.00 19.92  ? 548 HOH A O   1 
HETATM 4626 O  O   . HOH J 6 .   ? 0.021   -10.956 20.577  1.00 43.04  ? 549 HOH A O   1 
HETATM 4627 O  O   . HOH J 6 .   ? -20.520 -7.523  6.945   1.00 35.23  ? 550 HOH A O   1 
HETATM 4628 O  O   . HOH J 6 .   ? -20.487 -9.029  -0.360  1.00 27.70  ? 551 HOH A O   1 
HETATM 4629 O  O   . HOH J 6 .   ? 4.541   22.119  -1.640  1.00 19.96  ? 552 HOH A O   1 
HETATM 4630 O  O   . HOH J 6 .   ? -2.862  -15.118 14.532  1.00 23.21  ? 553 HOH A O   1 
HETATM 4631 O  O   . HOH J 6 .   ? -1.491  -13.660 -20.895 1.00 18.10  ? 554 HOH A O   1 
HETATM 4632 O  O   . HOH J 6 .   ? -18.163 -7.625  -0.737  1.00 27.74  ? 555 HOH A O   1 
HETATM 4633 O  O   . HOH J 6 .   ? -14.430 -4.903  8.053   1.00 24.19  ? 556 HOH A O   1 
HETATM 4634 O  O   . HOH J 6 .   ? -2.118  -20.351 5.437   1.00 16.99  ? 557 HOH A O   1 
HETATM 4635 O  O   . HOH J 6 .   ? 1.817   4.643   -15.048 1.00 15.08  ? 558 HOH A O   1 
HETATM 4636 O  O   . HOH J 6 .   ? 13.754  1.222   -10.618 1.00 21.24  ? 559 HOH A O   1 
HETATM 4637 O  O   . HOH J 6 .   ? -1.345  -18.021 -10.905 1.00 37.10  ? 560 HOH A O   1 
HETATM 4638 O  O   . HOH J 6 .   ? 13.576  1.030   12.092  1.00 28.61  ? 561 HOH A O   1 
HETATM 4639 O  O   . HOH J 6 .   ? 12.732  -9.953  1.909   1.00 24.74  ? 562 HOH A O   1 
HETATM 4640 O  O   . HOH J 6 .   ? -11.361 0.326   -13.631 1.00 17.47  ? 563 HOH A O   1 
HETATM 4641 O  O   . HOH J 6 .   ? 8.527   -18.193 -3.629  1.00 46.40  ? 564 HOH A O   1 
HETATM 4642 O  O   . HOH J 6 .   ? 2.752   9.828   -12.810 1.00 25.31  ? 565 HOH A O   1 
HETATM 4643 O  O   . HOH J 6 .   ? -3.344  -3.446  -21.685 1.00 18.62  ? 566 HOH A O   1 
HETATM 4644 O  O   . HOH J 6 .   ? 6.240   -8.032  -17.104 1.00 17.94  ? 567 HOH A O   1 
HETATM 4645 O  O   . HOH J 6 .   ? -1.277  17.260  3.785   1.00 22.41  ? 568 HOH A O   1 
HETATM 4646 O  O   . HOH J 6 .   ? -11.845 -15.977 2.223   1.00 33.22  ? 569 HOH A O   1 
HETATM 4647 O  O   . HOH J 6 .   ? 12.135  5.672   18.993  1.00 22.89  ? 570 HOH A O   1 
HETATM 4648 O  O   . HOH J 6 .   ? -7.425  -16.226 -15.260 1.00 23.86  ? 571 HOH A O   1 
HETATM 4649 O  O   . HOH J 6 .   ? 10.279  15.854  -12.672 1.00 39.07  ? 572 HOH A O   1 
HETATM 4650 O  O   . HOH J 6 .   ? 4.681   8.043   -16.834 1.00 34.40  ? 573 HOH A O   1 
HETATM 4651 O  O   . HOH J 6 .   ? -1.463  12.616  9.006   1.00 28.00  ? 574 HOH A O   1 
HETATM 4652 O  O   . HOH J 6 .   ? -3.510  -6.956  23.113  1.00 32.26  ? 575 HOH A O   1 
HETATM 4653 O  O   . HOH J 6 .   ? 0.330   -10.748 -24.228 1.00 35.08  ? 576 HOH A O   1 
HETATM 4654 O  O   . HOH J 6 .   ? 18.280  1.688   9.488   1.00 32.64  ? 577 HOH A O   1 
HETATM 4655 O  O   . HOH J 6 .   ? -14.775 0.792   21.230  1.00 32.22  ? 578 HOH A O   1 
HETATM 4656 O  O   . HOH J 6 .   ? -8.114  -10.451 -7.063  1.00 8.98   ? 579 HOH A O   1 
HETATM 4657 O  O   . HOH J 6 .   ? -18.712 -2.714  -7.948  1.00 24.17  ? 580 HOH A O   1 
HETATM 4658 O  O   . HOH J 6 .   ? -3.893  -17.962 -8.254  1.00 34.21  ? 581 HOH A O   1 
HETATM 4659 O  O   . HOH J 6 .   ? -9.639  -6.682  -16.880 1.00 22.30  ? 582 HOH A O   1 
HETATM 4660 O  O   . HOH J 6 .   ? -1.295  -8.434  17.221  1.00 30.98  ? 583 HOH A O   1 
HETATM 4661 O  O   . HOH J 6 .   ? -13.692 1.408   10.411  1.00 32.81  ? 584 HOH A O   1 
HETATM 4662 O  O   . HOH J 6 .   ? -9.956  -12.296 -6.465  1.00 30.23  ? 585 HOH A O   1 
HETATM 4663 O  O   . HOH J 6 .   ? -16.563 -3.997  9.295   1.00 31.54  ? 586 HOH A O   1 
HETATM 4664 O  O   . HOH J 6 .   ? -24.139 4.145   -7.229  1.00 30.59  ? 587 HOH A O   1 
HETATM 4665 O  O   . HOH J 6 .   ? 5.088   -18.495 -6.942  1.00 37.46  ? 588 HOH A O   1 
HETATM 4666 O  O   . HOH J 6 .   ? -16.262 -6.567  10.735  1.00 48.73  ? 589 HOH A O   1 
HETATM 4667 O  O   . HOH J 6 .   ? -0.972  -3.962  -20.104 1.00 17.90  ? 590 HOH A O   1 
HETATM 4668 O  O   . HOH J 6 .   ? 13.106  10.091  12.476  1.00 35.65  ? 591 HOH A O   1 
HETATM 4669 O  O   . HOH J 6 .   ? -0.574  -6.080  -18.250 1.00 20.24  ? 592 HOH A O   1 
HETATM 4670 O  O   . HOH J 6 .   ? 4.867   -14.041 -9.365  1.00 30.15  ? 593 HOH A O   1 
HETATM 4671 O  O   . HOH J 6 .   ? 0.969   13.854  8.621   1.00 26.23  ? 594 HOH A O   1 
HETATM 4672 O  O   . HOH J 6 .   ? -20.575 8.776   0.381   1.00 38.53  ? 595 HOH A O   1 
HETATM 4673 O  O   . HOH J 6 .   ? -20.255 -0.728  2.033   1.00 26.70  ? 596 HOH A O   1 
HETATM 4674 O  O   . HOH J 6 .   ? 14.549  -7.900  13.820  1.00 25.25  ? 597 HOH A O   1 
HETATM 4675 O  O   . HOH J 6 .   ? -13.019 2.923   18.099  1.00 42.47  ? 598 HOH A O   1 
HETATM 4676 O  O   . HOH J 6 .   ? 10.930  -11.082 17.754  1.00 28.10  ? 599 HOH A O   1 
HETATM 4677 O  O   . HOH J 6 .   ? 17.728  7.557   -3.561  1.00 36.66  ? 600 HOH A O   1 
HETATM 4678 O  O   . HOH J 6 .   ? -17.739 8.051   -5.892  1.00 17.11  ? 601 HOH A O   1 
HETATM 4679 O  O   . HOH J 6 .   ? -1.985  -17.717 -5.997  1.00 16.53  ? 602 HOH A O   1 
HETATM 4680 O  O   . HOH J 6 .   ? -9.326  20.263  -6.756  1.00 69.48  ? 603 HOH A O   1 
HETATM 4681 O  O   . HOH J 6 .   ? 6.751   1.035   -24.040 1.00 32.10  ? 604 HOH A O   1 
HETATM 4682 O  O   . HOH J 6 .   ? -7.173  -12.889 -17.168 1.00 35.31  ? 605 HOH A O   1 
HETATM 4683 O  O   . HOH J 6 .   ? 3.932   5.677   -17.325 1.00 25.99  ? 606 HOH A O   1 
HETATM 4684 O  O   . HOH J 6 .   ? 2.685   5.464   22.810  1.00 36.38  ? 607 HOH A O   1 
HETATM 4685 O  O   . HOH J 6 .   ? -8.784  13.397  -10.238 1.00 22.44  ? 608 HOH A O   1 
HETATM 4686 O  O   . HOH J 6 .   ? 7.214   -4.872  -26.419 1.00 35.95  ? 609 HOH A O   1 
HETATM 4687 O  O   . HOH J 6 .   ? -15.276 -8.879  -2.522  1.00 38.32  ? 610 HOH A O   1 
HETATM 4688 O  O   . HOH J 6 .   ? -8.343  10.415  -14.781 1.00 31.06  ? 611 HOH A O   1 
HETATM 4689 O  O   . HOH J 6 .   ? 7.791   -10.084 -15.590 1.00 29.74  ? 612 HOH A O   1 
HETATM 4690 O  O   . HOH J 6 .   ? 2.601   9.063   -15.210 1.00 52.49  ? 613 HOH A O   1 
HETATM 4691 O  O   . HOH J 6 .   ? -9.645  -1.070  -23.760 1.00 53.22  ? 614 HOH A O   1 
HETATM 4692 O  O   . HOH J 6 .   ? 17.791  7.687   0.710   1.00 48.16  ? 615 HOH A O   1 
HETATM 4693 O  O   . HOH J 6 .   ? 0.360   -21.979 3.716   1.00 24.23  ? 616 HOH A O   1 
HETATM 4694 O  O   . HOH J 6 .   ? 2.709   -15.454 -1.072  1.00 13.06  ? 617 HOH A O   1 
HETATM 4695 O  O   . HOH J 6 .   ? 0.215   22.675  -9.354  1.00 29.83  ? 618 HOH A O   1 
HETATM 4696 O  O   . HOH J 6 .   ? -4.732  5.125   21.751  1.00 34.39  ? 619 HOH A O   1 
HETATM 4697 O  O   . HOH J 6 .   ? -4.646  -14.082 -19.050 1.00 40.98  ? 620 HOH A O   1 
HETATM 4698 O  O   . HOH J 6 .   ? -25.126 -9.055  0.945   1.00 45.08  ? 621 HOH A O   1 
HETATM 4699 O  O   . HOH J 6 .   ? 16.180  -4.443  10.899  1.00 38.13  ? 622 HOH A O   1 
HETATM 4700 O  O   . HOH J 6 .   ? -2.122  -3.235  -24.036 1.00 38.03  ? 623 HOH A O   1 
HETATM 4701 O  O   . HOH J 6 .   ? -13.208 4.565   15.832  1.00 29.90  ? 624 HOH A O   1 
HETATM 4702 O  O   . HOH J 6 .   ? 7.427   21.772  -1.580  1.00 23.13  ? 625 HOH A O   1 
HETATM 4703 O  O   . HOH J 6 .   ? -21.521 -4.851  8.628   1.00 49.86  ? 626 HOH A O   1 
HETATM 4704 O  O   . HOH J 6 .   ? 5.080   19.376  11.923  1.00 45.42  ? 627 HOH A O   1 
HETATM 4705 O  O   . HOH J 6 .   ? -1.603  -15.653 -19.158 1.00 19.76  ? 628 HOH A O   1 
HETATM 4706 O  O   . HOH J 6 .   ? -10.448 2.326   22.693  1.00 38.74  ? 629 HOH A O   1 
HETATM 4707 O  O   . HOH J 6 .   ? 12.572  -7.870  -9.487  1.00 23.98  ? 630 HOH A O   1 
HETATM 4708 O  O   . HOH J 6 .   ? 9.617   -12.221 -8.981  1.00 41.35  ? 631 HOH A O   1 
HETATM 4709 O  O   . HOH J 6 .   ? -1.322  -20.045 7.784   1.00 33.30  ? 632 HOH A O   1 
HETATM 4710 O  O   . HOH J 6 .   ? -15.092 -1.323  9.745   1.00 51.27  ? 633 HOH A O   1 
HETATM 4711 O  O   . HOH J 6 .   ? -24.592 1.990   0.800   1.00 28.96  ? 634 HOH A O   1 
HETATM 4712 O  O   . HOH J 6 .   ? -11.863 -7.962  -13.699 1.00 39.20  ? 635 HOH A O   1 
HETATM 4713 O  O   . HOH J 6 .   ? -6.234  7.450   6.021   1.00 57.44  ? 636 HOH A O   1 
HETATM 4714 O  O   . HOH J 6 .   ? -13.006 -11.696 7.829   1.00 27.50  ? 637 HOH A O   1 
HETATM 4715 O  O   . HOH J 6 .   ? -8.887  -11.227 -11.319 1.00 25.62  ? 638 HOH A O   1 
HETATM 4716 O  O   . HOH J 6 .   ? -2.499  -15.617 -16.409 1.00 38.83  ? 639 HOH A O   1 
HETATM 4717 O  O   . HOH J 6 .   ? 14.828  11.184  -10.190 1.00 38.41  ? 640 HOH A O   1 
HETATM 4718 O  O   . HOH J 6 .   ? 6.677   -16.534 -4.640  1.00 28.65  ? 641 HOH A O   1 
HETATM 4719 O  O   . HOH J 6 .   ? -8.412  -15.569 -9.690  1.00 24.33  ? 642 HOH A O   1 
HETATM 4720 O  O   . HOH J 6 .   ? 11.008  1.816   17.641  1.00 37.41  ? 643 HOH A O   1 
HETATM 4721 O  O   . HOH J 6 .   ? -10.987 4.577   14.120  1.00 39.31  ? 644 HOH A O   1 
HETATM 4722 O  O   . HOH J 6 .   ? -10.606 19.560  -8.873  1.00 34.13  ? 645 HOH A O   1 
HETATM 4723 O  O   . HOH J 6 .   ? 7.154   -12.021 -21.941 1.00 26.12  ? 646 HOH A O   1 
HETATM 4724 O  O   . HOH J 6 .   ? 9.912   -0.283  -27.252 1.00 36.37  ? 647 HOH A O   1 
HETATM 4725 O  O   . HOH J 6 .   ? -4.328  22.270  -10.497 1.00 31.28  ? 648 HOH A O   1 
HETATM 4726 O  O   . HOH J 6 .   ? -25.572 -2.112  -9.155  1.00 25.04  ? 649 HOH A O   1 
HETATM 4727 O  O   . HOH J 6 .   ? -4.304  11.149  6.269   1.00 24.03  ? 650 HOH A O   1 
HETATM 4728 O  O   . HOH J 6 .   ? -16.441 -9.312  0.324   1.00 35.69  ? 651 HOH A O   1 
HETATM 4729 O  O   . HOH J 6 .   ? -5.324  22.446  -5.922  1.00 23.11  ? 652 HOH A O   1 
HETATM 4730 O  O   . HOH J 6 .   ? 16.735  -4.741  4.276   1.00 29.79  ? 653 HOH A O   1 
HETATM 4731 O  O   . HOH J 6 .   ? -8.180  -9.839  -15.808 1.00 29.12  ? 654 HOH A O   1 
HETATM 4732 O  O   . HOH J 6 .   ? -8.792  -11.303 -17.507 1.00 39.33  ? 655 HOH A O   1 
HETATM 4733 O  O   . HOH J 6 .   ? 13.763  -5.618  15.585  1.00 39.02  ? 656 HOH A O   1 
HETATM 4734 O  O   . HOH J 6 .   ? 6.674   -12.142 -10.477 1.00 19.62  ? 657 HOH A O   1 
HETATM 4735 O  O   . HOH J 6 .   ? -12.077 -12.341 -4.905  1.00 27.97  ? 658 HOH A O   1 
HETATM 4736 O  O   . HOH J 6 .   ? -16.404 -4.231  12.654  1.00 40.65  ? 659 HOH A O   1 
HETATM 4737 O  O   . HOH J 6 .   ? -5.092  -7.878  -17.838 1.00 27.21  ? 660 HOH A O   1 
HETATM 4738 O  O   . HOH J 6 .   ? 4.393   24.577  -2.923  1.00 15.28  ? 661 HOH A O   1 
HETATM 4739 O  O   . HOH J 6 .   ? -12.200 14.593  -6.885  1.00 39.28  ? 662 HOH A O   1 
HETATM 4740 O  O   . HOH J 6 .   ? 12.209  14.114  -11.199 1.00 50.85  ? 663 HOH A O   1 
HETATM 4741 O  O   . HOH J 6 .   ? -8.198  -15.854 10.720  1.00 37.23  ? 664 HOH A O   1 
HETATM 4742 O  O   . HOH J 6 .   ? -16.717 -2.058  26.648  1.00 20.49  ? 665 HOH A O   1 
HETATM 4743 O  O   . HOH J 6 .   ? -2.201  -8.809  20.155  1.00 40.11  ? 666 HOH A O   1 
HETATM 4744 O  O   . HOH J 6 .   ? -5.381  -6.067  24.288  1.00 42.52  ? 667 HOH A O   1 
HETATM 4745 O  O   . HOH J 6 .   ? 12.297  -10.595 -9.012  1.00 38.42  ? 668 HOH A O   1 
HETATM 4746 O  O   . HOH J 6 .   ? 6.349   -12.802 -13.068 1.00 38.72  ? 669 HOH A O   1 
HETATM 4747 O  O   . HOH J 6 .   ? -11.735 -15.864 8.587   1.00 32.00  ? 670 HOH A O   1 
HETATM 4748 O  O   . HOH J 6 .   ? 1.169   -9.681  18.874  1.00 42.91  ? 671 HOH A O   1 
HETATM 4749 O  O   . HOH J 6 .   ? -16.438 7.155   -13.558 1.00 35.58  ? 672 HOH A O   1 
HETATM 4750 O  O   . HOH J 6 .   ? -8.894  -9.225  -13.253 1.00 22.03  ? 673 HOH A O   1 
HETATM 4751 O  O   . HOH J 6 .   ? 5.923   19.251  -9.979  1.00 39.13  ? 674 HOH A O   1 
HETATM 4752 O  O   . HOH J 6 .   ? -12.568 11.450  -10.521 1.00 29.86  ? 675 HOH A O   1 
HETATM 4753 O  O   . HOH J 6 .   ? 8.974   0.664   18.679  1.00 45.72  ? 676 HOH A O   1 
HETATM 4754 O  O   . HOH J 6 .   ? -13.555 -10.255 -7.233  1.00 49.88  ? 677 HOH A O   1 
HETATM 4755 O  O   . HOH J 6 .   ? -11.890 4.955   20.833  1.00 34.16  ? 678 HOH A O   1 
HETATM 4756 O  O   . HOH J 6 .   ? -17.062 -6.965  25.088  1.00 26.55  ? 679 HOH A O   1 
HETATM 4757 O  O   . HOH J 6 .   ? -13.748 10.626  -6.428  1.00 24.27  ? 680 HOH A O   1 
HETATM 4758 O  O   . HOH J 6 .   ? -6.274  -13.782 18.203  1.00 27.86  ? 681 HOH A O   1 
HETATM 4759 O  O   . HOH J 6 .   ? -18.837 -11.210 -0.296  1.00 32.63  ? 682 HOH A O   1 
HETATM 4760 O  O   . HOH J 6 .   ? -15.889 4.072   19.199  1.00 36.25  ? 683 HOH A O   1 
HETATM 4761 O  O   . HOH J 6 .   ? -6.925  -4.420  23.942  1.00 26.16  ? 684 HOH A O   1 
HETATM 4762 O  O   . HOH J 6 .   ? 9.748   -13.737 -6.752  1.00 44.30  ? 685 HOH A O   1 
HETATM 4763 O  O   . HOH J 6 .   ? -12.163 13.782  -10.313 1.00 34.57  ? 686 HOH A O   1 
HETATM 4764 O  O   . HOH J 6 .   ? -3.988  -16.480 12.666  1.00 29.95  ? 687 HOH A O   1 
HETATM 4765 O  O   . HOH J 6 .   ? 2.694   -17.672 -10.506 1.00 25.55  ? 688 HOH A O   1 
HETATM 4766 O  O   . HOH J 6 .   ? -7.979  -15.006 -18.651 1.00 32.94  ? 689 HOH A O   1 
HETATM 4767 O  O   . HOH J 6 .   ? 16.551  0.636   -10.125 1.00 25.83  ? 690 HOH A O   1 
HETATM 4768 O  O   . HOH J 6 .   ? -16.900 10.346  -2.705  1.00 36.23  ? 691 HOH A O   1 
HETATM 4769 O  O   . HOH J 6 .   ? -9.777  14.501  1.970   1.00 38.42  ? 692 HOH A O   1 
HETATM 4770 O  O   . HOH J 6 .   ? -7.577  -21.613 1.525   1.00 35.18  ? 693 HOH A O   1 
HETATM 4771 O  O   . HOH J 6 .   ? -25.021 -4.940  7.842   1.00 37.64  ? 694 HOH A O   1 
HETATM 4772 O  O   . HOH J 6 .   ? -5.186  -5.619  -21.939 1.00 37.28  ? 695 HOH A O   1 
HETATM 4773 O  O   . HOH J 6 .   ? -22.129 2.454   -12.842 1.00 34.11  ? 696 HOH A O   1 
HETATM 4774 O  O   . HOH J 6 .   ? -14.330 -4.803  -17.849 1.00 58.16  ? 697 HOH A O   1 
HETATM 4775 O  O   . HOH J 6 .   ? -13.589 11.303  1.921   1.00 47.24  ? 698 HOH A O   1 
HETATM 4776 O  O   . HOH J 6 .   ? -24.305 0.392   -12.613 1.00 31.90  ? 699 HOH A O   1 
HETATM 4777 O  O   . HOH J 6 .   ? -15.872 10.661  -11.048 1.00 36.12  ? 700 HOH A O   1 
HETATM 4778 O  O   . HOH J 6 .   ? -15.470 11.531  -0.888  1.00 36.58  ? 701 HOH A O   1 
HETATM 4779 O  O   . HOH J 6 .   ? -11.990 12.326  0.679   1.00 64.16  ? 702 HOH A O   1 
HETATM 4780 O  O   . HOH J 6 .   ? -6.688  11.344  5.372   1.00 46.86  ? 703 HOH A O   1 
HETATM 4781 O  O   . HOH K 6 .   ? -3.925  7.636   21.735  1.00 49.06  ? 401 HOH B O   1 
HETATM 4782 O  O   . HOH K 6 .   ? -36.224 15.809  45.425  1.00 357.51 ? 402 HOH B O   1 
HETATM 4783 O  O   . HOH K 6 .   ? 5.138   15.797  27.704  1.00 27.85  ? 403 HOH B O   1 
HETATM 4784 O  O   . HOH K 6 .   ? -10.985 5.006   34.049  1.00 29.68  ? 404 HOH B O   1 
HETATM 4785 O  O   . HOH K 6 .   ? -9.339  19.217  2.854   1.00 38.22  ? 405 HOH B O   1 
HETATM 4786 O  O   . HOH K 6 .   ? -29.425 39.892  21.898  1.00 28.74  ? 406 HOH B O   1 
HETATM 4787 O  O   . HOH K 6 .   ? -30.847 15.443  13.684  1.00 49.21  ? 407 HOH B O   1 
HETATM 4788 O  O   . HOH K 6 .   ? -5.747  13.175  10.042  1.00 33.97  ? 408 HOH B O   1 
HETATM 4789 O  O   . HOH K 6 .   ? -20.202 9.975   55.938  1.00 33.34  ? 409 HOH B O   1 
HETATM 4790 O  O   . HOH K 6 .   ? -5.253  18.523  18.948  1.00 35.44  ? 410 HOH B O   1 
HETATM 4791 O  O   . HOH K 6 .   ? -6.516  8.407   28.675  1.00 34.99  ? 411 HOH B O   1 
HETATM 4792 O  O   . HOH K 6 .   ? -24.266 5.891   44.985  1.00 20.38  ? 412 HOH B O   1 
HETATM 4793 O  O   . HOH K 6 .   ? -20.373 44.281  36.002  1.00 24.26  ? 413 HOH B O   1 
HETATM 4794 O  O   . HOH K 6 .   ? -30.226 31.084  45.944  1.00 29.37  ? 414 HOH B O   1 
HETATM 4795 O  O   . HOH K 6 .   ? -22.693 4.187   48.117  1.00 24.41  ? 415 HOH B O   1 
HETATM 4796 O  O   . HOH K 6 .   ? -16.162 17.687  9.396   1.00 31.84  ? 416 HOH B O   1 
HETATM 4797 O  O   . HOH K 6 .   ? -33.807 19.665  44.973  1.00 27.79  ? 417 HOH B O   1 
HETATM 4798 O  O   . HOH K 6 .   ? -23.972 13.543  10.602  1.00 34.16  ? 418 HOH B O   1 
HETATM 4799 O  O   . HOH K 6 .   ? -9.804  8.237   46.948  1.00 44.34  ? 419 HOH B O   1 
HETATM 4800 O  O   . HOH K 6 .   ? -16.003 10.984  52.568  1.00 34.76  ? 420 HOH B O   1 
HETATM 4801 O  O   . HOH K 6 .   ? -12.984 2.912   22.287  1.00 26.53  ? 421 HOH B O   1 
HETATM 4802 O  O   . HOH K 6 .   ? 1.860   22.353  32.050  1.00 26.16  ? 422 HOH B O   1 
HETATM 4803 O  O   . HOH K 6 .   ? 5.382   19.988  30.401  1.00 23.52  ? 423 HOH B O   1 
HETATM 4804 O  O   . HOH K 6 .   ? -8.841  13.331  10.527  1.00 38.90  ? 424 HOH B O   1 
HETATM 4805 O  O   . HOH K 6 .   ? -11.154 18.417  31.591  1.00 7.81   ? 425 HOH B O   1 
HETATM 4806 O  O   . HOH K 6 .   ? -22.294 35.026  45.106  1.00 31.49  ? 426 HOH B O   1 
HETATM 4807 O  O   . HOH K 6 .   ? -7.425  9.113   21.042  1.00 19.33  ? 427 HOH B O   1 
HETATM 4808 O  O   . HOH K 6 .   ? -25.785 11.824  11.366  1.00 49.52  ? 428 HOH B O   1 
HETATM 4809 O  O   . HOH K 6 .   ? -28.273 24.814  56.361  1.00 47.65  ? 429 HOH B O   1 
HETATM 4810 O  O   . HOH K 6 .   ? -8.789  36.982  40.516  1.00 34.50  ? 430 HOH B O   1 
HETATM 4811 O  O   . HOH K 6 .   ? -24.074 1.030   19.275  1.00 33.60  ? 431 HOH B O   1 
HETATM 4812 O  O   . HOH K 6 .   ? 3.345   22.820  40.324  1.00 24.83  ? 432 HOH B O   1 
HETATM 4813 O  O   . HOH K 6 .   ? -13.732 29.212  22.348  1.00 26.10  ? 433 HOH B O   1 
HETATM 4814 O  O   . HOH K 6 .   ? -5.546  19.072  42.473  1.00 18.90  ? 434 HOH B O   1 
HETATM 4815 O  O   . HOH K 6 .   ? -7.231  17.991  23.620  1.00 20.98  ? 435 HOH B O   1 
HETATM 4816 O  O   . HOH K 6 .   ? -24.977 0.742   29.202  1.00 30.42  ? 436 HOH B O   1 
HETATM 4817 O  O   . HOH K 6 .   ? -6.302  27.580  45.787  1.00 17.21  ? 437 HOH B O   1 
HETATM 4818 O  O   . HOH K 6 .   ? -35.228 33.675  35.690  1.00 36.94  ? 438 HOH B O   1 
HETATM 4819 O  O   . HOH K 6 .   ? -21.555 11.125  12.997  1.00 31.52  ? 439 HOH B O   1 
HETATM 4820 O  O   . HOH K 6 .   ? -23.583 6.022   15.917  1.00 96.17  ? 440 HOH B O   1 
HETATM 4821 O  O   . HOH K 6 .   ? -33.663 4.652   22.503  1.00 53.41  ? 441 HOH B O   1 
HETATM 4822 O  O   . HOH K 6 .   ? -20.908 2.774   23.544  1.00 29.64  ? 442 HOH B O   1 
HETATM 4823 O  O   . HOH K 6 .   ? -25.284 31.425  13.727  1.00 33.19  ? 443 HOH B O   1 
HETATM 4824 O  O   . HOH K 6 .   ? -11.617 17.600  8.839   1.00 45.04  ? 444 HOH B O   1 
HETATM 4825 O  O   . HOH K 6 .   ? -28.648 40.287  34.529  1.00 24.42  ? 445 HOH B O   1 
HETATM 4826 O  O   . HOH K 6 .   ? -18.967 28.551  44.836  1.00 20.22  ? 446 HOH B O   1 
HETATM 4827 O  O   . HOH K 6 .   ? -23.705 33.038  43.580  1.00 15.79  ? 447 HOH B O   1 
HETATM 4828 O  O   . HOH K 6 .   ? -27.799 32.971  27.128  1.00 23.47  ? 448 HOH B O   1 
HETATM 4829 O  O   . HOH K 6 .   ? -34.746 14.749  24.944  1.00 19.53  ? 449 HOH B O   1 
HETATM 4830 O  O   . HOH K 6 .   ? -6.526  8.550   9.335   1.00 22.17  ? 450 HOH B O   1 
HETATM 4831 O  O   . HOH K 6 .   ? -20.277 4.220   33.264  1.00 12.95  ? 451 HOH B O   1 
HETATM 4832 O  O   . HOH K 6 .   ? -26.728 37.074  49.183  1.00 29.55  ? 452 HOH B O   1 
HETATM 4833 O  O   . HOH K 6 .   ? -20.530 31.264  41.286  1.00 8.91   ? 453 HOH B O   1 
HETATM 4834 O  O   . HOH K 6 .   ? -30.496 41.464  29.665  1.00 22.89  ? 454 HOH B O   1 
HETATM 4835 O  O   . HOH K 6 .   ? -29.134 1.550   21.277  1.00 30.83  ? 455 HOH B O   1 
HETATM 4836 O  O   . HOH K 6 .   ? -0.174  14.200  19.491  1.00 40.58  ? 456 HOH B O   1 
HETATM 4837 O  O   . HOH K 6 .   ? -7.995  6.763   25.290  1.00 19.37  ? 457 HOH B O   1 
HETATM 4838 O  O   . HOH K 6 .   ? -11.018 31.756  43.928  1.00 16.85  ? 458 HOH B O   1 
HETATM 4839 O  O   . HOH K 6 .   ? -25.891 38.531  39.351  1.00 19.44  ? 459 HOH B O   1 
HETATM 4840 O  O   . HOH K 6 .   ? -10.187 21.441  11.076  1.00 19.31  ? 460 HOH B O   1 
HETATM 4841 O  O   . HOH K 6 .   ? -10.466 33.194  39.537  1.00 19.20  ? 461 HOH B O   1 
HETATM 4842 O  O   . HOH K 6 .   ? -9.984  23.664  50.438  1.00 32.16  ? 462 HOH B O   1 
HETATM 4843 O  O   . HOH K 6 .   ? -29.858 18.313  57.177  1.00 37.02  ? 463 HOH B O   1 
HETATM 4844 O  O   . HOH K 6 .   ? -33.228 19.480  22.737  1.00 22.94  ? 464 HOH B O   1 
HETATM 4845 O  O   . HOH K 6 .   ? -8.355  30.813  44.155  1.00 26.73  ? 465 HOH B O   1 
HETATM 4846 O  O   . HOH K 6 .   ? -17.015 7.684   47.583  1.00 20.44  ? 466 HOH B O   1 
HETATM 4847 O  O   . HOH K 6 .   ? -14.644 10.591  48.133  1.00 22.86  ? 467 HOH B O   1 
HETATM 4848 O  O   . HOH K 6 .   ? -28.524 1.857   31.004  1.00 34.73  ? 468 HOH B O   1 
HETATM 4849 O  O   . HOH K 6 .   ? -14.420 9.011   34.062  1.00 7.30   ? 469 HOH B O   1 
HETATM 4850 O  O   . HOH K 6 .   ? -9.653  2.778   26.745  1.00 31.08  ? 470 HOH B O   1 
HETATM 4851 O  O   . HOH K 6 .   ? -32.809 16.433  18.677  1.00 24.53  ? 471 HOH B O   1 
HETATM 4852 O  O   . HOH K 6 .   ? -6.656  25.034  23.923  1.00 39.56  ? 472 HOH B O   1 
HETATM 4853 O  O   . HOH K 6 .   ? -17.658 29.854  25.018  1.00 22.31  ? 473 HOH B O   1 
HETATM 4854 O  O   . HOH K 6 .   ? -17.842 6.901   27.417  1.00 8.90   ? 474 HOH B O   1 
HETATM 4855 O  O   . HOH K 6 .   ? -32.113 4.009   29.518  1.00 23.29  ? 475 HOH B O   1 
HETATM 4856 O  O   . HOH K 6 .   ? -36.066 25.942  31.346  1.00 34.78  ? 476 HOH B O   1 
HETATM 4857 O  O   . HOH K 6 .   ? 0.641   13.141  24.845  1.00 36.96  ? 477 HOH B O   1 
HETATM 4858 O  O   . HOH K 6 .   ? -5.586  20.104  44.977  1.00 23.89  ? 478 HOH B O   1 
HETATM 4859 O  O   . HOH K 6 .   ? -35.596 32.011  29.077  1.00 45.14  ? 479 HOH B O   1 
HETATM 4860 O  O   . HOH K 6 .   ? -33.845 31.290  35.927  1.00 23.51  ? 480 HOH B O   1 
HETATM 4861 O  O   . HOH K 6 .   ? -35.553 7.183   23.705  1.00 28.81  ? 481 HOH B O   1 
HETATM 4862 O  O   . HOH K 6 .   ? -12.458 13.856  45.114  1.00 10.29  ? 482 HOH B O   1 
HETATM 4863 O  O   . HOH K 6 .   ? -15.308 31.364  22.899  1.00 23.52  ? 483 HOH B O   1 
HETATM 4864 O  O   . HOH K 6 .   ? -26.930 14.103  36.289  1.00 8.69   ? 484 HOH B O   1 
HETATM 4865 O  O   . HOH K 6 .   ? -9.113  33.688  36.121  1.00 32.82  ? 485 HOH B O   1 
HETATM 4866 O  O   . HOH K 6 .   ? -8.754  10.779  41.130  1.00 22.49  ? 486 HOH B O   1 
HETATM 4867 O  O   . HOH K 6 .   ? -31.458 15.453  39.385  1.00 15.99  ? 487 HOH B O   1 
HETATM 4868 O  O   . HOH K 6 .   ? -10.038 36.415  32.436  1.00 23.91  ? 488 HOH B O   1 
HETATM 4869 O  O   . HOH K 6 .   ? -27.805 1.915   23.921  1.00 15.65  ? 489 HOH B O   1 
HETATM 4870 O  O   . HOH K 6 .   ? -13.364 11.367  36.883  1.00 8.09   ? 490 HOH B O   1 
HETATM 4871 O  O   . HOH K 6 .   ? -30.139 33.445  42.281  1.00 19.13  ? 491 HOH B O   1 
HETATM 4872 O  O   . HOH K 6 .   ? -6.599  13.651  42.545  1.00 35.29  ? 492 HOH B O   1 
HETATM 4873 O  O   . HOH K 6 .   ? -10.012 1.921   30.893  1.00 44.14  ? 493 HOH B O   1 
HETATM 4874 O  O   . HOH K 6 .   ? -27.075 8.585   53.676  1.00 31.41  ? 494 HOH B O   1 
HETATM 4875 O  O   . HOH K 6 .   ? -31.776 28.178  20.589  1.00 24.41  ? 495 HOH B O   1 
HETATM 4876 O  O   . HOH K 6 .   ? -16.521 43.634  35.590  1.00 14.67  ? 496 HOH B O   1 
HETATM 4877 O  O   . HOH K 6 .   ? -13.645 6.664   40.485  1.00 12.07  ? 497 HOH B O   1 
HETATM 4878 O  O   . HOH K 6 .   ? -14.174 14.174  47.113  1.00 18.23  ? 498 HOH B O   1 
HETATM 4879 O  O   . HOH K 6 .   ? -18.383 22.975  9.337   1.00 30.12  ? 499 HOH B O   1 
HETATM 4880 O  O   . HOH K 6 .   ? -23.178 42.481  30.548  1.00 31.61  ? 500 HOH B O   1 
HETATM 4881 O  O   . HOH K 6 .   ? -29.889 6.069   37.004  1.00 34.87  ? 501 HOH B O   1 
HETATM 4882 O  O   . HOH K 6 .   ? -1.347  18.726  37.004  1.00 16.77  ? 502 HOH B O   1 
HETATM 4883 O  O   . HOH K 6 .   ? -32.893 7.792   32.185  1.00 37.64  ? 503 HOH B O   1 
HETATM 4884 O  O   . HOH K 6 .   ? -28.653 18.674  13.320  1.00 25.65  ? 504 HOH B O   1 
HETATM 4885 O  O   . HOH K 6 .   ? -4.631  29.688  36.499  1.00 17.95  ? 505 HOH B O   1 
HETATM 4886 O  O   . HOH K 6 .   ? -34.392 27.145  24.370  1.00 33.78  ? 506 HOH B O   1 
HETATM 4887 O  O   . HOH K 6 .   ? -17.239 5.667   17.306  1.00 21.30  ? 507 HOH B O   1 
HETATM 4888 O  O   . HOH K 6 .   ? -24.524 42.811  33.402  1.00 21.47  ? 508 HOH B O   1 
HETATM 4889 O  O   . HOH K 6 .   ? -27.764 27.036  12.017  1.00 57.23  ? 509 HOH B O   1 
HETATM 4890 O  O   . HOH K 6 .   ? -19.157 35.931  26.030  1.00 22.55  ? 510 HOH B O   1 
HETATM 4891 O  O   . HOH K 6 .   ? -25.979 10.186  40.330  1.00 13.04  ? 511 HOH B O   1 
HETATM 4892 O  O   . HOH K 6 .   ? -13.953 9.294   12.877  1.00 21.86  ? 512 HOH B O   1 
HETATM 4893 O  O   . HOH K 6 .   ? -19.492 28.752  9.223   1.00 44.31  ? 513 HOH B O   1 
HETATM 4894 O  O   . HOH K 6 .   ? -17.300 13.886  48.537  1.00 14.66  ? 514 HOH B O   1 
HETATM 4895 O  O   . HOH K 6 .   ? -33.395 11.414  33.128  1.00 25.30  ? 515 HOH B O   1 
HETATM 4896 O  O   . HOH K 6 .   ? -1.919  13.174  32.503  1.00 22.22  ? 516 HOH B O   1 
HETATM 4897 O  O   . HOH K 6 .   ? -38.338 22.239  22.525  1.00 34.89  ? 517 HOH B O   1 
HETATM 4898 O  O   . HOH K 6 .   ? -27.676 14.795  55.050  1.00 46.54  ? 518 HOH B O   1 
HETATM 4899 O  O   . HOH K 6 .   ? -26.537 6.998   48.635  1.00 34.53  ? 519 HOH B O   1 
HETATM 4900 O  O   . HOH K 6 .   ? -41.016 10.258  37.657  1.00 45.77  ? 520 HOH B O   1 
HETATM 4901 O  O   . HOH K 6 .   ? -28.496 34.890  28.610  1.00 22.23  ? 521 HOH B O   1 
HETATM 4902 O  O   . HOH K 6 .   ? -10.931 40.487  32.209  1.00 44.87  ? 522 HOH B O   1 
HETATM 4903 O  O   . HOH K 6 .   ? -14.740 38.593  28.339  1.00 23.97  ? 523 HOH B O   1 
HETATM 4904 O  O   . HOH K 6 .   ? -13.270 9.340   41.162  1.00 9.79   ? 524 HOH B O   1 
HETATM 4905 O  O   . HOH K 6 .   ? -23.234 3.969   30.638  1.00 19.53  ? 525 HOH B O   1 
HETATM 4906 O  O   . HOH K 6 .   ? -33.272 9.127   27.336  1.00 19.04  ? 526 HOH B O   1 
HETATM 4907 O  O   . HOH K 6 .   ? -27.306 6.049   37.840  1.00 24.54  ? 527 HOH B O   1 
HETATM 4908 O  O   . HOH K 6 .   ? -1.659  25.719  43.668  1.00 31.62  ? 528 HOH B O   1 
HETATM 4909 O  O   . HOH K 6 .   ? -34.463 1.865   24.858  1.00 36.29  ? 529 HOH B O   1 
HETATM 4910 O  O   . HOH K 6 .   ? -36.092 25.288  36.801  1.00 26.96  ? 530 HOH B O   1 
HETATM 4911 O  O   . HOH K 6 .   ? -18.687 33.127  22.832  1.00 31.85  ? 531 HOH B O   1 
HETATM 4912 O  O   . HOH K 6 .   ? -24.983 2.232   38.595  1.00 32.60  ? 532 HOH B O   1 
HETATM 4913 O  O   . HOH K 6 .   ? -22.720 13.469  12.722  1.00 29.16  ? 533 HOH B O   1 
HETATM 4914 O  O   . HOH K 6 .   ? -33.229 22.484  50.368  1.00 41.23  ? 534 HOH B O   1 
HETATM 4915 O  O   . HOH K 6 .   ? -5.003  17.625  36.905  1.00 15.88  ? 535 HOH B O   1 
HETATM 4916 O  O   . HOH K 6 .   ? -35.778 29.101  42.884  1.00 33.58  ? 536 HOH B O   1 
HETATM 4917 O  O   . HOH K 6 .   ? -22.837 30.432  44.436  1.00 24.58  ? 537 HOH B O   1 
HETATM 4918 O  O   . HOH K 6 .   ? -14.688 6.411   16.648  1.00 40.39  ? 538 HOH B O   1 
HETATM 4919 O  O   . HOH K 6 .   ? -22.957 5.597   42.634  1.00 15.07  ? 539 HOH B O   1 
HETATM 4920 O  O   . HOH K 6 .   ? -5.635  15.776  23.736  1.00 23.49  ? 540 HOH B O   1 
HETATM 4921 O  O   . HOH K 6 .   ? -8.479  31.242  39.973  1.00 15.47  ? 541 HOH B O   1 
HETATM 4922 O  O   . HOH K 6 .   ? -21.956 25.287  46.855  1.00 15.08  ? 542 HOH B O   1 
HETATM 4923 O  O   . HOH K 6 .   ? -21.037 23.735  49.334  1.00 22.30  ? 543 HOH B O   1 
HETATM 4924 O  O   . HOH K 6 .   ? -7.305  10.909  25.491  1.00 21.39  ? 544 HOH B O   1 
HETATM 4925 O  O   . HOH K 6 .   ? -4.917  15.157  38.223  1.00 26.41  ? 545 HOH B O   1 
HETATM 4926 O  O   . HOH K 6 .   ? -10.638 14.052  48.543  1.00 24.25  ? 546 HOH B O   1 
HETATM 4927 O  O   . HOH K 6 .   ? -8.466  16.251  50.422  1.00 26.11  ? 547 HOH B O   1 
HETATM 4928 O  O   . HOH K 6 .   ? -6.850  23.344  13.801  1.00 46.30  ? 548 HOH B O   1 
HETATM 4929 O  O   . HOH K 6 .   ? -23.808 36.974  42.989  1.00 24.71  ? 549 HOH B O   1 
HETATM 4930 O  O   . HOH K 6 .   ? -33.746 21.718  19.759  1.00 27.60  ? 550 HOH B O   1 
HETATM 4931 O  O   . HOH K 6 .   ? -16.646 17.258  53.427  1.00 19.36  ? 551 HOH B O   1 
HETATM 4932 O  O   . HOH K 6 .   ? -33.292 22.362  47.936  1.00 37.59  ? 552 HOH B O   1 
HETATM 4933 O  O   . HOH K 6 .   ? 3.968   24.699  38.783  1.00 31.88  ? 553 HOH B O   1 
HETATM 4934 O  O   . HOH K 6 .   ? -18.971 12.326  14.613  1.00 32.16  ? 554 HOH B O   1 
HETATM 4935 O  O   . HOH K 6 .   ? -29.264 32.561  24.720  1.00 19.68  ? 555 HOH B O   1 
HETATM 4936 O  O   . HOH K 6 .   ? -23.442 21.562  9.869   1.00 35.96  ? 556 HOH B O   1 
HETATM 4937 O  O   . HOH K 6 .   ? -12.194 26.455  23.883  1.00 34.81  ? 557 HOH B O   1 
HETATM 4938 O  O   . HOH K 6 .   ? -3.029  18.932  46.014  1.00 31.53  ? 558 HOH B O   1 
HETATM 4939 O  O   . HOH K 6 .   ? -18.706 37.937  27.961  1.00 23.57  ? 559 HOH B O   1 
HETATM 4940 O  O   . HOH K 6 .   ? -24.998 6.607   40.992  1.00 33.31  ? 560 HOH B O   1 
HETATM 4941 O  O   . HOH K 6 .   ? -32.777 10.791  29.894  1.00 23.35  ? 561 HOH B O   1 
HETATM 4942 O  O   . HOH K 6 .   ? -8.700  20.999  45.423  1.00 13.41  ? 562 HOH B O   1 
HETATM 4943 O  O   . HOH K 6 .   ? -17.873 0.296   26.352  1.00 16.53  ? 563 HOH B O   1 
HETATM 4944 O  O   . HOH K 6 .   ? -33.842 21.901  42.380  1.00 20.27  ? 564 HOH B O   1 
HETATM 4945 O  O   . HOH K 6 .   ? -12.369 3.199   37.581  1.00 37.45  ? 565 HOH B O   1 
HETATM 4946 O  O   . HOH K 6 .   ? -8.258  4.540   29.809  1.00 31.41  ? 566 HOH B O   1 
HETATM 4947 O  O   . HOH K 6 .   ? -19.049 16.804  51.875  1.00 21.39  ? 567 HOH B O   1 
HETATM 4948 O  O   . HOH K 6 .   ? -35.942 25.477  50.308  1.00 40.54  ? 568 HOH B O   1 
HETATM 4949 O  O   . HOH K 6 .   ? -30.376 36.477  44.466  1.00 54.29  ? 569 HOH B O   1 
HETATM 4950 O  O   . HOH K 6 .   ? 1.359   23.711  41.868  1.00 28.31  ? 570 HOH B O   1 
HETATM 4951 O  O   . HOH K 6 .   ? -10.163 8.166   38.180  1.00 19.12  ? 571 HOH B O   1 
HETATM 4952 O  O   . HOH K 6 .   ? -26.354 12.582  48.853  1.00 20.66  ? 572 HOH B O   1 
HETATM 4953 O  O   . HOH K 6 .   ? -31.174 2.852   22.609  1.00 29.50  ? 573 HOH B O   1 
HETATM 4954 O  O   . HOH K 6 .   ? -11.101 41.321  39.194  1.00 33.21  ? 574 HOH B O   1 
HETATM 4955 O  O   . HOH K 6 .   ? -36.007 29.255  18.767  1.00 34.11  ? 575 HOH B O   1 
HETATM 4956 O  O   . HOH K 6 .   ? 4.902   12.029  30.797  1.00 38.95  ? 576 HOH B O   1 
HETATM 4957 O  O   . HOH K 6 .   ? -11.955 10.206  38.854  1.00 8.92   ? 577 HOH B O   1 
HETATM 4958 O  O   . HOH K 6 .   ? -20.533 40.159  28.128  1.00 25.73  ? 578 HOH B O   1 
HETATM 4959 O  O   . HOH K 6 .   ? -15.981 2.686   39.947  1.00 30.87  ? 579 HOH B O   1 
HETATM 4960 O  O   . HOH K 6 .   ? -22.889 26.173  9.042   1.00 39.05  ? 580 HOH B O   1 
HETATM 4961 O  O   . HOH K 6 .   ? -19.519 14.586  50.039  1.00 22.61  ? 581 HOH B O   1 
HETATM 4962 O  O   . HOH K 6 .   ? -18.079 3.085   37.723  1.00 17.42  ? 582 HOH B O   1 
HETATM 4963 O  O   . HOH K 6 .   ? -16.914 24.197  51.057  1.00 20.97  ? 583 HOH B O   1 
HETATM 4964 O  O   . HOH K 6 .   ? -1.424  17.964  39.667  1.00 26.78  ? 584 HOH B O   1 
HETATM 4965 O  O   . HOH K 6 .   ? -4.831  11.701  34.484  1.00 39.09  ? 585 HOH B O   1 
HETATM 4966 O  O   . HOH K 6 .   ? -23.340 41.428  27.372  1.00 34.65  ? 586 HOH B O   1 
HETATM 4967 O  O   . HOH K 6 .   ? -24.749 28.683  48.694  1.00 42.66  ? 587 HOH B O   1 
HETATM 4968 O  O   . HOH K 6 .   ? -2.291  28.719  37.667  1.00 15.73  ? 588 HOH B O   1 
HETATM 4969 O  O   . HOH K 6 .   ? 3.182   16.783  40.324  1.00 26.25  ? 589 HOH B O   1 
HETATM 4970 O  O   . HOH K 6 .   ? -21.156 34.626  22.978  1.00 27.76  ? 590 HOH B O   1 
HETATM 4971 O  O   . HOH K 6 .   ? -12.967 7.904   48.806  1.00 38.04  ? 591 HOH B O   1 
HETATM 4972 O  O   . HOH K 6 .   ? 0.443   11.595  32.182  1.00 28.66  ? 592 HOH B O   1 
HETATM 4973 O  O   . HOH K 6 .   ? 3.082   18.685  29.377  1.00 28.60  ? 593 HOH B O   1 
HETATM 4974 O  O   . HOH K 6 .   ? -11.905 30.821  46.668  1.00 32.40  ? 594 HOH B O   1 
HETATM 4975 O  O   . HOH K 6 .   ? -34.602 12.833  17.838  1.00 27.04  ? 595 HOH B O   1 
HETATM 4976 O  O   . HOH K 6 .   ? -11.379 23.739  25.462  1.00 34.74  ? 596 HOH B O   1 
HETATM 4977 O  O   . HOH K 6 .   ? -31.963 8.046   34.875  1.00 53.15  ? 597 HOH B O   1 
HETATM 4978 O  O   . HOH K 6 .   ? -3.552  16.574  22.333  1.00 32.28  ? 598 HOH B O   1 
HETATM 4979 O  O   . HOH K 6 .   ? -16.002 27.331  9.932   1.00 36.73  ? 599 HOH B O   1 
HETATM 4980 O  O   . HOH K 6 .   ? -31.114 9.606   14.023  1.00 26.13  ? 600 HOH B O   1 
HETATM 4981 O  O   . HOH K 6 .   ? -4.288  9.277   27.460  1.00 40.73  ? 601 HOH B O   1 
HETATM 4982 O  O   . HOH K 6 .   ? -16.570 2.803   21.012  1.00 36.19  ? 602 HOH B O   1 
HETATM 4983 O  O   . HOH K 6 .   ? -11.243 34.095  41.983  1.00 25.31  ? 603 HOH B O   1 
HETATM 4984 O  O   . HOH K 6 .   ? -17.360 13.299  13.470  1.00 25.75  ? 604 HOH B O   1 
HETATM 4985 O  O   . HOH K 6 .   ? -22.781 5.253   32.868  1.00 13.64  ? 605 HOH B O   1 
HETATM 4986 O  O   . HOH K 6 .   ? -22.599 29.894  46.611  1.00 41.65  ? 606 HOH B O   1 
HETATM 4987 O  O   . HOH K 6 .   ? -26.777 21.687  55.928  1.00 37.75  ? 607 HOH B O   1 
HETATM 4988 O  O   . HOH K 6 .   ? -10.811 19.248  55.458  1.00 48.61  ? 608 HOH B O   1 
HETATM 4989 O  O   . HOH K 6 .   ? -15.359 9.556   10.184  1.00 38.83  ? 609 HOH B O   1 
HETATM 4990 O  O   . HOH K 6 .   ? -5.302  21.460  10.489  1.00 28.95  ? 610 HOH B O   1 
HETATM 4991 O  O   . HOH K 6 .   ? -9.686  23.035  9.028   1.00 36.54  ? 611 HOH B O   1 
HETATM 4992 O  O   . HOH K 6 .   ? -36.423 16.078  20.995  1.00 34.08  ? 612 HOH B O   1 
HETATM 4993 O  O   . HOH K 6 .   ? 1.309   15.819  23.053  1.00 32.10  ? 613 HOH B O   1 
HETATM 4994 O  O   . HOH K 6 .   ? -28.389 13.476  50.416  1.00 38.94  ? 614 HOH B O   1 
HETATM 4995 O  O   . HOH K 6 .   ? -33.664 19.098  19.913  1.00 32.86  ? 615 HOH B O   1 
HETATM 4996 O  O   . HOH K 6 .   ? -3.100  13.696  6.622   1.00 26.50  ? 616 HOH B O   1 
HETATM 4997 O  O   . HOH K 6 .   ? -7.525  13.957  6.691   1.00 38.82  ? 617 HOH B O   1 
HETATM 4998 O  O   . HOH K 6 .   ? -18.604 0.720   24.232  1.00 32.51  ? 618 HOH B O   1 
HETATM 4999 O  O   . HOH K 6 .   ? -9.731  14.936  8.436   1.00 42.05  ? 619 HOH B O   1 
HETATM 5000 O  O   . HOH K 6 .   ? -27.508 42.365  33.346  1.00 27.31  ? 620 HOH B O   1 
HETATM 5001 O  O   . HOH K 6 .   ? -29.703 8.494   40.662  1.00 43.83  ? 621 HOH B O   1 
HETATM 5002 O  O   . HOH K 6 .   ? -32.619 12.773  41.317  1.00 25.08  ? 622 HOH B O   1 
HETATM 5003 O  O   . HOH K 6 .   ? -38.371 28.886  32.005  1.00 49.80  ? 623 HOH B O   1 
HETATM 5004 O  O   . HOH K 6 .   ? -7.384  16.481  4.156   1.00 37.29  ? 624 HOH B O   1 
HETATM 5005 O  O   . HOH K 6 .   ? -19.160 32.212  9.588   1.00 35.94  ? 625 HOH B O   1 
HETATM 5006 O  O   . HOH K 6 .   ? -7.098  8.946   23.829  1.00 23.23  ? 626 HOH B O   1 
HETATM 5007 O  O   . HOH K 6 .   ? -3.322  18.576  5.110   1.00 20.27  ? 627 HOH B O   1 
HETATM 5008 O  O   . HOH K 6 .   ? -11.316 9.479   43.051  1.00 26.89  ? 628 HOH B O   1 
HETATM 5009 O  O   . HOH K 6 .   ? -5.700  10.779  39.309  1.00 41.52  ? 629 HOH B O   1 
HETATM 5010 O  O   . HOH K 6 .   ? -4.398  13.595  23.043  1.00 53.77  ? 630 HOH B O   1 
HETATM 5011 O  O   . HOH K 6 .   ? -2.848  18.341  15.013  1.00 33.14  ? 631 HOH B O   1 
HETATM 5012 O  O   . HOH K 6 .   ? -9.038  25.294  17.730  1.00 40.80  ? 632 HOH B O   1 
HETATM 5013 O  O   . HOH K 6 .   ? -26.592 5.007   40.455  1.00 44.99  ? 633 HOH B O   1 
HETATM 5014 O  O   . HOH K 6 .   ? -17.451 5.067   48.221  1.00 35.50  ? 634 HOH B O   1 
HETATM 5015 O  O   . HOH K 6 .   ? -30.988 22.403  14.148  1.00 36.04  ? 635 HOH B O   1 
HETATM 5016 O  O   . HOH K 6 .   ? -26.687 4.100   36.518  1.00 28.18  ? 636 HOH B O   1 
HETATM 5017 O  O   . HOH K 6 .   ? -8.570  12.395  45.036  1.00 40.26  ? 637 HOH B O   1 
HETATM 5018 O  O   . HOH K 6 .   ? 0.560   27.851  28.578  1.00 35.06  ? 638 HOH B O   1 
HETATM 5019 O  O   . HOH K 6 .   ? -20.448 27.514  46.812  1.00 19.72  ? 639 HOH B O   1 
HETATM 5020 O  O   . HOH K 6 .   ? 5.399   18.638  41.056  1.00 21.51  ? 640 HOH B O   1 
HETATM 5021 O  O   . HOH K 6 .   ? -23.842 26.316  48.990  1.00 29.02  ? 641 HOH B O   1 
HETATM 5022 O  O   . HOH K 6 .   ? -11.127 9.421   49.141  1.00 34.28  ? 642 HOH B O   1 
HETATM 5023 O  O   . HOH K 6 .   ? -22.996 41.690  24.739  1.00 34.06  ? 643 HOH B O   1 
HETATM 5024 O  O   . HOH K 6 .   ? -37.273 15.669  23.819  1.00 33.18  ? 644 HOH B O   1 
HETATM 5025 O  O   . HOH K 6 .   ? -15.924 32.014  25.491  1.00 23.89  ? 645 HOH B O   1 
HETATM 5026 O  O   . HOH K 6 .   ? -14.832 43.014  37.661  1.00 31.04  ? 646 HOH B O   1 
HETATM 5027 O  O   . HOH K 6 .   ? -26.176 39.493  42.202  1.00 34.26  ? 647 HOH B O   1 
HETATM 5028 O  O   . HOH K 6 .   ? -38.666 14.427  45.302  1.00 33.50  ? 648 HOH B O   1 
HETATM 5029 O  O   . HOH K 6 .   ? -11.741 4.973   41.578  1.00 25.57  ? 649 HOH B O   1 
HETATM 5030 O  O   . HOH K 6 .   ? -25.224 39.211  19.213  1.00 41.13  ? 650 HOH B O   1 
HETATM 5031 O  O   . HOH K 6 .   ? -5.603  9.438   37.514  1.00 30.87  ? 651 HOH B O   1 
HETATM 5032 O  O   . HOH K 6 .   ? -14.861 12.853  49.384  1.00 27.04  ? 652 HOH B O   1 
HETATM 5033 O  O   . HOH K 6 .   ? -27.802 10.532  47.476  1.00 31.42  ? 653 HOH B O   1 
HETATM 5034 O  O   . HOH K 6 .   ? -12.019 10.901  47.646  1.00 28.69  ? 654 HOH B O   1 
HETATM 5035 O  O   . HOH K 6 .   ? -7.018  23.296  9.552   1.00 31.62  ? 655 HOH B O   1 
HETATM 5036 O  O   . HOH K 6 .   ? -8.021  9.453   7.145   1.00 43.72  ? 656 HOH B O   1 
HETATM 5037 O  O   . HOH K 6 .   ? 5.495   21.410  41.880  1.00 22.52  ? 657 HOH B O   1 
HETATM 5038 O  O   . HOH K 6 .   ? -33.156 40.036  37.205  1.00 42.21  ? 658 HOH B O   1 
HETATM 5039 O  O   . HOH K 6 .   ? -30.028 20.383  58.901  1.00 35.58  ? 659 HOH B O   1 
HETATM 5040 O  O   . HOH K 6 .   ? -3.628  11.518  31.523  1.00 33.12  ? 660 HOH B O   1 
HETATM 5041 O  O   . HOH K 6 .   ? -24.480 45.237  34.714  1.00 16.13  ? 661 HOH B O   1 
HETATM 5042 O  O   . HOH K 6 .   ? -15.278 5.371   12.175  1.00 60.89  ? 662 HOH B O   1 
HETATM 5043 O  O   . HOH K 6 .   ? -26.763 8.554   42.347  1.00 22.58  ? 663 HOH B O   1 
HETATM 5044 O  O   . HOH K 6 .   ? -2.811  20.631  12.911  1.00 32.11  ? 664 HOH B O   1 
HETATM 5045 O  O   . HOH K 6 .   ? -8.149  12.981  47.528  1.00 35.28  ? 665 HOH B O   1 
HETATM 5046 O  O   . HOH K 6 .   ? -33.987 15.059  16.136  1.00 44.45  ? 666 HOH B O   1 
HETATM 5047 O  O   . HOH K 6 .   ? -13.179 28.286  26.062  1.00 42.26  ? 667 HOH B O   1 
HETATM 5048 O  O   . HOH K 6 .   ? -1.854  16.456  16.360  1.00 35.52  ? 668 HOH B O   1 
HETATM 5049 O  O   . HOH K 6 .   ? -22.346 40.163  22.978  1.00 40.02  ? 669 HOH B O   1 
HETATM 5050 O  O   . HOH K 6 .   ? -7.817  35.264  38.353  1.00 32.85  ? 670 HOH B O   1 
HETATM 5051 O  O   . HOH K 6 .   ? -32.384 10.134  40.904  1.00 32.79  ? 671 HOH B O   1 
HETATM 5052 O  O   . HOH K 6 .   ? -7.953  8.438   36.703  1.00 30.91  ? 672 HOH B O   1 
HETATM 5053 O  O   . HOH K 6 .   ? -11.877 6.378   9.655   1.00 34.78  ? 673 HOH B O   1 
HETATM 5054 O  O   . HOH K 6 .   ? -17.475 12.163  11.336  1.00 32.12  ? 674 HOH B O   1 
HETATM 5055 O  O   . HOH K 6 .   ? -8.377  4.788   23.135  1.00 30.53  ? 675 HOH B O   1 
HETATM 5056 O  O   . HOH K 6 .   ? -11.134 11.458  45.001  1.00 16.48  ? 676 HOH B O   1 
HETATM 5057 O  O   . HOH K 6 .   ? 2.247   26.557  43.329  1.00 36.47  ? 677 HOH B O   1 
HETATM 5058 O  O   . HOH K 6 .   ? -26.529 8.208   44.763  1.00 44.83  ? 678 HOH B O   1 
HETATM 5059 O  O   . HOH K 6 .   ? -3.963  22.300  14.799  1.00 46.71  ? 679 HOH B O   1 
HETATM 5060 O  O   . HOH K 6 .   ? -6.905  25.163  15.798  1.00 30.62  ? 680 HOH B O   1 
HETATM 5061 O  O   . HOH K 6 .   ? -4.934  26.068  19.783  1.00 37.33  ? 681 HOH B O   1 
HETATM 5062 O  O   . HOH K 6 .   ? -3.097  19.958  16.683  1.00 39.97  ? 682 HOH B O   1 
HETATM 5063 O  O   . HOH K 6 .   ? -12.400 -0.812  30.369  1.00 36.21  ? 683 HOH B O   1 
HETATM 5064 O  O   . HOH K 6 .   ? -7.388  32.248  42.196  1.00 31.84  ? 684 HOH B O   1 
HETATM 5065 O  O   . HOH K 6 .   ? -6.318  31.378  38.214  1.00 24.03  ? 685 HOH B O   1 
HETATM 5066 O  O   . HOH K 6 .   ? -34.344 24.886  57.562  1.00 36.89  ? 686 HOH B O   1 
HETATM 5067 O  O   . HOH K 6 .   ? -13.835 6.890   13.675  1.00 30.29  ? 687 HOH B O   1 
HETATM 5068 O  O   . HOH K 6 .   ? -3.228  31.082  34.542  1.00 37.02  ? 688 HOH B O   1 
HETATM 5069 O  O   . HOH K 6 .   ? -22.839 2.951   42.192  1.00 22.17  ? 689 HOH B O   1 
HETATM 5070 O  O   . HOH K 6 .   ? -10.174 30.701  29.841  1.00 39.33  ? 690 HOH B O   1 
HETATM 5071 O  O   . HOH K 6 .   ? -34.627 6.309   19.832  1.00 31.75  ? 691 HOH B O   1 
HETATM 5072 O  O   . HOH K 6 .   ? -14.961 15.154  53.770  1.00 34.14  ? 692 HOH B O   1 
HETATM 5073 O  O   . HOH K 6 .   ? -24.922 2.135   41.238  1.00 40.93  ? 693 HOH B O   1 
HETATM 5074 O  O   . HOH K 6 .   ? 1.902   23.329  44.460  1.00 38.15  ? 694 HOH B O   1 
HETATM 5075 O  O   . HOH K 6 .   ? 3.907   27.308  41.027  1.00 37.28  ? 695 HOH B O   1 
HETATM 5076 O  O   . HOH K 6 .   ? -4.191  31.639  42.141  1.00 45.86  ? 696 HOH B O   1 
HETATM 5077 O  O   . HOH K 6 .   ? 2.523   17.836  20.503  1.00 37.94  ? 697 HOH B O   1 
HETATM 5078 O  O   . HOH K 6 .   ? -21.868 36.219  17.605  1.00 35.11  ? 698 HOH B O   1 
HETATM 5079 O  O   . HOH K 6 .   ? -1.670  24.323  15.834  1.00 51.90  ? 699 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 4   ? 0.2750 0.8290 1.0025 -0.2059 0.3314  -0.3447 4   HIS A N   
2    C  CA  . HIS A 4   ? 0.5651 0.5008 0.8490 0.0692  0.2614  -0.3177 4   HIS A CA  
3    C  C   . HIS A 4   ? 0.1818 0.3633 0.4440 -0.2267 0.1269  -0.1368 4   HIS A C   
4    O  O   . HIS A 4   ? 0.1416 0.3385 0.4106 -0.0168 0.1426  -0.0409 4   HIS A O   
5    C  CB  . HIS A 4   ? 0.4039 0.9807 0.8986 -0.5378 0.1179  -0.4439 4   HIS A CB  
6    C  CG  . HIS A 4   ? 1.0642 0.7634 0.8743 0.3405  -0.3150 -0.4543 4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.9092 1.0892 0.8022 0.5430  -0.1483 -0.2947 4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.9125 0.9958 1.1075 0.3614  -0.3643 -0.4132 4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 1.2938 1.8144 0.5666 0.3976  -0.1342 -0.4907 4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.7125 1.5864 1.0170 0.4080  -0.4564 -0.5213 4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.1093 0.2838 0.4093 -0.0162 0.1289  -0.0583 5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1399 0.2239 0.3619 0.0179  0.1014  -0.0334 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1312 0.2545 0.3177 0.0115  0.1584  -0.0089 5   TRP A C   
14   O  O   . TRP A 5   ? 0.1280 0.2272 0.3586 0.0084  0.1588  -0.0096 5   TRP A O   
15   C  CB  . TRP A 5   ? 0.0620 0.2749 0.3703 -0.0239 0.0485  0.0143  5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1032 0.2125 0.2395 -0.0190 0.0901  -0.0625 5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2404 0.2196 0.3291 -0.0490 0.0895  -0.0665 5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.0694 0.2172 0.2526 -0.0466 0.1005  -0.0370 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2312 0.1769 0.2879 -0.0363 0.0785  -0.0705 5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1251 0.2311 0.2418 -0.0293 0.0488  -0.0304 5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.0809 0.2267 0.2046 0.0052  0.1030  -0.0124 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1305 0.2130 0.1861 -0.0576 -0.0062 -0.0306 5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.0757 0.1945 0.2355 -0.0298 0.1072  -0.0055 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1194 0.2238 0.2026 -0.0511 0.0747  0.0033  5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.0723 0.1935 0.3282 -0.0221 0.1341  -0.0061 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1622 0.1870 0.3018 0.0170  0.1226  -0.0013 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.0499 0.1721 0.3476 -0.0183 0.1212  -0.0269 6   GLY A C   
28   O  O   . GLY A 6   ? 0.0578 0.1855 0.3570 -0.0232 0.1299  0.0026  6   GLY A O   
29   N  N   . TYR A 7   ? 0.0708 0.1611 0.4005 -0.0237 0.1306  -0.0358 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.0822 0.1779 0.4889 0.0108  0.1345  -0.0430 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.1407 0.3592 0.6014 -0.1136 0.1943  0.0673  7   TYR A C   
32   O  O   . TYR A 7   ? 0.4517 0.1945 0.8266 -0.1167 0.1741  0.0273  7   TYR A O   
33   C  CB  . TYR A 7   ? 0.0825 0.2087 0.5366 0.0006  0.1991  0.0459  7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.0708 0.1414 0.2097 -0.0320 0.0628  0.0043  7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.0298 0.1474 0.2446 -0.0043 0.0735  0.0189  7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.0942 0.1478 0.2150 -0.0021 0.0605  -0.0172 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.0217 0.1205 0.2052 -0.0360 0.0366  -0.0282 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1350 0.1658 0.1771 -0.0179 0.0572  -0.0121 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.0662 0.1227 0.1671 -0.0268 0.0361  -0.0294 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.0928 0.1274 0.1868 -0.0482 0.0310  -0.0421 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.0766 0.2481 0.7871 -0.0405 0.1758  0.0117  8   GLY A N   
42   C  CA  . GLY A 8   ? 0.2439 0.1211 0.8083 -0.0403 0.2410  0.0304  8   GLY A CA  
43   C  C   . GLY A 8   ? 0.5771 0.2447 0.9417 -0.0883 0.2982  -0.2736 8   GLY A C   
44   O  O   . GLY A 8   ? 0.6549 0.4657 0.4795 -0.0040 -0.0840 0.1604  8   GLY A O   
45   N  N   . LYS A 9   ? 0.4537 0.1905 0.9165 -0.0476 0.3236  -0.0456 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.4279 0.3122 0.9006 -0.0886 0.2318  0.0068  9   LYS A CA  
47   C  C   . LYS A 9   ? 0.2497 0.4465 0.5874 -0.0826 -0.0297 -0.0870 9   LYS A C   
48   O  O   . LYS A 9   ? 0.1518 0.3441 0.6148 0.0244  0.1368  0.0167  9   LYS A O   
49   C  CB  . LYS A 9   ? 0.3158 0.6485 1.4548 -0.1113 0.1559  -0.2682 9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.6013 0.4601 0.7605 -0.0390 0.0496  -0.0109 9   LYS A CG  
51   N  N   . HIS A 10  ? 0.3571 0.3579 0.8681 -0.0762 0.3907  -0.0842 10  HIS A N   
52   C  CA  . HIS A 10  ? 0.2357 0.5250 0.5712 0.0861  0.3219  -0.1132 10  HIS A CA  
53   C  C   . HIS A 10  ? 0.8572 0.8482 1.3685 -0.3888 0.0635  0.0234  10  HIS A C   
54   O  O   . HIS A 10  ? 0.4975 0.6380 0.5075 -0.0858 0.0365  -0.4010 10  HIS A O   
55   C  CB  . HIS A 10  ? 0.1970 0.7288 0.4684 -0.3710 0.0279  -0.0394 10  HIS A CB  
56   C  CG  . HIS A 10  ? 0.1120 0.2046 0.3513 -0.1069 0.0467  -0.0108 10  HIS A CG  
57   N  ND1 . HIS A 10  ? 0.0983 0.2982 0.4138 -0.1083 0.0717  -0.0209 10  HIS A ND1 
58   C  CD2 . HIS A 10  ? 0.1761 0.2210 0.3509 -0.0594 0.1872  -0.0036 10  HIS A CD2 
59   C  CE1 . HIS A 10  ? 0.1937 0.1991 0.2990 -0.1323 0.0075  -0.0798 10  HIS A CE1 
60   N  NE2 . HIS A 10  ? 0.0969 0.2831 0.3095 -0.0732 0.0441  0.0067  10  HIS A NE2 
61   N  N   . ASN A 11  ? 1.3332 1.0887 1.1705 -0.7813 0.6200  -0.8344 11  ASN A N   
62   C  CA  . ASN A 11  ? 0.2075 0.3788 0.7171 -0.0840 0.3331  0.0921  11  ASN A CA  
63   C  C   . ASN A 11  ? 0.1631 0.3780 0.4526 -0.1778 0.1655  0.0270  11  ASN A C   
64   O  O   . ASN A 11  ? 0.1027 0.1683 0.4124 -0.0675 0.1780  -0.0307 11  ASN A O   
65   C  CB  . ASN A 11  ? 0.3051 0.3949 0.8268 0.1872  0.1976  -0.1480 11  ASN A CB  
66   C  CG  . ASN A 11  ? 0.5729 0.2882 0.5768 0.1152  0.1585  -0.1747 11  ASN A CG  
67   O  OD1 . ASN A 11  ? 0.2381 0.1989 0.5220 0.0078  0.1987  -0.0072 11  ASN A OD1 
68   N  ND2 . ASN A 11  ? 0.1992 0.2629 0.4875 0.0011  0.1926  -0.0089 11  ASN A ND2 
69   N  N   . GLY A 12  ? 0.1639 0.3652 0.5237 -0.1509 0.2267  -0.0149 12  GLY A N   
70   C  CA  . GLY A 12  ? 0.0896 0.3072 0.3412 -0.0674 0.1554  -0.0212 12  GLY A CA  
71   C  C   . GLY A 12  ? 0.0541 0.1860 0.3604 -0.0012 0.0890  -0.0469 12  GLY A C   
72   O  O   . GLY A 12  ? 0.0479 0.1620 0.4241 -0.0732 0.0890  -0.0795 12  GLY A O   
73   N  N   . PRO A 13  ? 0.0255 0.1316 0.2744 -0.0322 0.0490  -0.0383 13  PRO A N   
74   C  CA  . PRO A 13  ? 0.0261 0.1516 0.3248 -0.0379 0.0624  -0.0261 13  PRO A CA  
75   C  C   . PRO A 13  ? 0.0156 0.1586 0.4408 -0.0331 0.0381  -0.0388 13  PRO A C   
76   O  O   . PRO A 13  ? 0.0138 0.1848 0.3379 -0.0317 0.0262  -0.0098 13  PRO A O   
77   C  CB  . PRO A 13  ? 0.0490 0.1953 0.2969 0.0078  0.1104  0.0244  13  PRO A CB  
78   C  CG  . PRO A 13  ? 0.0433 0.1535 0.2557 -0.0232 0.0939  -0.0216 13  PRO A CG  
79   C  CD  . PRO A 13  ? 0.0421 0.1763 0.2874 -0.0413 0.0817  0.0126  13  PRO A CD  
80   N  N   . GLU A 14  ? 0.0492 0.1449 0.3548 -0.0674 0.0887  -0.0669 14  GLU A N   
81   C  CA  . GLU A 14  ? 0.0448 0.1601 0.6335 -0.0710 -0.0288 -0.0633 14  GLU A CA  
82   C  C   . GLU A 14  ? 0.0596 0.1720 0.4307 -0.0817 0.0739  0.0000  14  GLU A C   
83   O  O   . GLU A 14  ? 0.0511 0.1940 0.4356 -0.0668 -0.0259 -0.0629 14  GLU A O   
84   C  CB  . GLU A 14  ? 0.2105 0.1242 0.5101 -0.1134 -0.0375 -0.0947 14  GLU A CB  
85   C  CG  . GLU A 14  ? 0.1203 0.2836 0.5705 -0.0879 0.0625  -0.0226 14  GLU A CG  
86   C  CD  . GLU A 14  ? 0.3784 0.4453 0.4474 -0.0965 0.0201  0.0465  14  GLU A CD  
87   O  OE1 . GLU A 14  ? 0.4151 0.5981 0.6160 0.0156  0.1732  0.0927  14  GLU A OE1 
88   O  OE2 . GLU A 14  ? 0.5635 0.6912 0.6598 0.0823  -0.2370 0.0996  14  GLU A OE2 
89   N  N   . HIS A 15  ? 0.0382 0.1828 0.4696 -0.0649 0.0642  -0.0099 15  HIS A N   
90   C  CA  . HIS A 15  ? 0.1300 0.1110 0.5468 -0.0055 -0.0133 -0.0974 15  HIS A CA  
91   C  C   . HIS A 15  ? 0.9102 1.1303 3.0824 -0.7580 -0.2623 -0.9902 15  HIS A C   
92   O  O   . HIS A 15  ? 0.9822 1.0661 1.6793 -0.5033 0.3240  0.2197  15  HIS A O   
93   C  CB  . HIS A 15  ? 0.0349 0.2837 0.5389 -0.0861 -0.0040 -0.0838 15  HIS A CB  
94   C  CG  . HIS A 15  ? 0.0693 0.1754 0.6298 -0.0907 0.1591  -0.1375 15  HIS A CG  
95   N  ND1 . HIS A 15  ? 0.0407 0.2788 0.5463 -0.0894 0.0851  -0.1055 15  HIS A ND1 
96   C  CD2 . HIS A 15  ? 0.0922 0.2102 0.5305 -0.1151 0.0712  -0.0834 15  HIS A CD2 
97   C  CE1 . HIS A 15  ? 0.3216 0.2631 0.4839 -0.0331 0.0495  -0.0124 15  HIS A CE1 
98   N  NE2 . HIS A 15  ? 0.1423 0.2375 0.5366 -0.1253 0.1385  -0.0232 15  HIS A NE2 
99   N  N   . TRP A 16  ? 0.0630 0.3174 0.4957 -0.0033 0.0184  -0.0595 16  TRP A N   
100  C  CA  . TRP A 16  ? 0.2227 0.6632 0.8808 -0.0068 0.3236  -0.2545 16  TRP A CA  
101  C  C   . TRP A 16  ? 0.0764 0.7838 0.6445 -0.2284 0.1082  -0.2296 16  TRP A C   
102  O  O   . TRP A 16  ? 0.0141 0.3439 0.4066 -0.0499 -0.0114 -0.0085 16  TRP A O   
103  C  CB  . TRP A 16  ? 0.0678 0.2066 0.3421 -0.0207 0.0361  -0.0301 16  TRP A CB  
104  C  CG  . TRP A 16  ? 0.0411 0.1600 0.3058 -0.0586 0.0644  -0.0095 16  TRP A CG  
105  C  CD1 . TRP A 16  ? 0.0973 0.1229 0.2062 -0.0449 0.0458  -0.0258 16  TRP A CD1 
106  C  CD2 . TRP A 16  ? 0.0338 0.1341 0.2796 -0.0319 0.0810  -0.0391 16  TRP A CD2 
107  N  NE1 . TRP A 16  ? 0.0412 0.1541 0.2506 -0.0413 0.0802  -0.0183 16  TRP A NE1 
108  C  CE2 . TRP A 16  ? 0.0351 0.1444 0.2679 -0.0460 0.0699  -0.0352 16  TRP A CE2 
109  C  CE3 . TRP A 16  ? 0.0397 0.1254 0.2845 -0.0439 0.0797  -0.0309 16  TRP A CE3 
110  C  CZ2 . TRP A 16  ? 0.0326 0.1649 0.2522 -0.0444 0.0625  -0.0161 16  TRP A CZ2 
111  C  CZ3 . TRP A 16  ? 0.0244 0.1150 0.2278 -0.0353 0.0510  -0.0448 16  TRP A CZ3 
112  C  CH2 . TRP A 16  ? 0.0259 0.1519 0.2122 -0.0313 0.0566  -0.0276 16  TRP A CH2 
113  N  N   . HIS A 17  ? 0.0237 0.1795 0.4033 -0.0119 0.0758  0.0525  17  HIS A N   
114  C  CA  . HIS A 17  ? 0.0195 0.1985 0.3043 -0.0412 0.0317  -0.0793 17  HIS A CA  
115  C  C   . HIS A 17  ? 0.0480 0.2321 0.4351 -0.0962 0.0464  -0.0725 17  HIS A C   
116  O  O   . HIS A 17  ? 0.0500 0.2804 0.4670 -0.0179 -0.0241 -0.0283 17  HIS A O   
117  C  CB  . HIS A 17  ? 0.0249 0.2477 0.3414 -0.0587 -0.0159 -0.0847 17  HIS A CB  
118  C  CG  . HIS A 17  ? 0.0281 0.2948 0.3849 -0.0674 -0.0222 -0.1005 17  HIS A CG  
119  N  ND1 . HIS A 17  ? 0.0886 0.1946 0.5352 -0.1244 0.0041  -0.0010 17  HIS A ND1 
120  C  CD2 . HIS A 17  ? 1.1586 1.8589 3.7240 -1.1406 1.1111  0.2837  17  HIS A CD2 
121  C  CE1 . HIS A 17  ? 0.3461 1.6945 1.4357 -0.6154 0.6305  -0.7567 17  HIS A CE1 
122  N  NE2 . HIS A 17  ? 0.8179 1.4434 1.3444 -0.6976 0.4514  -0.5956 17  HIS A NE2 
123  N  N   . LYS A 18  ? 0.0118 0.1801 0.4303 -0.0306 0.0049  -0.0562 18  LYS A N   
124  C  CA  . LYS A 18  ? 0.0075 0.1550 0.4434 -0.0101 0.0184  -0.0499 18  LYS A CA  
125  C  C   . LYS A 18  ? 0.1554 0.2439 0.5140 -0.0724 -0.0210 -0.1020 18  LYS A C   
126  O  O   . LYS A 18  ? 0.2606 0.2124 0.6411 0.1053  -0.0231 -0.0418 18  LYS A O   
127  C  CB  . LYS A 18  ? 0.0220 0.1578 0.4140 -0.0392 0.0084  -0.0585 18  LYS A CB  
128  C  CG  . LYS A 18  ? 0.0608 0.1973 0.4724 -0.0812 0.1149  -0.1050 18  LYS A CG  
129  C  CD  . LYS A 18  ? 0.0787 0.1949 0.5165 -0.0554 0.0740  -0.0434 18  LYS A CD  
130  C  CE  . LYS A 18  ? 0.1647 0.2055 0.3935 -0.0219 0.0298  -0.0820 18  LYS A CE  
131  N  NZ  . LYS A 18  ? 0.1346 0.4109 0.7144 -0.2253 0.1480  -0.1922 18  LYS A NZ  
132  N  N   . ASP A 19  ? 0.0247 0.1886 0.4950 -0.0499 0.0281  -0.1030 19  ASP A N   
133  C  CA  . ASP A 19  ? 0.0872 0.1285 0.4559 -0.0144 0.0478  -0.0926 19  ASP A CA  
134  C  C   . ASP A 19  ? 0.0730 0.1633 0.4662 -0.0376 0.0080  -0.0866 19  ASP A C   
135  O  O   . ASP A 19  ? 0.0615 0.1743 0.5383 -0.0223 0.0607  -0.0842 19  ASP A O   
136  C  CB  . ASP A 19  ? 0.0714 0.3282 0.4792 -0.0545 -0.0168 -0.0851 19  ASP A CB  
137  C  CG  . ASP A 19  ? 0.0904 0.2584 0.4860 -0.0201 -0.0278 0.0189  19  ASP A CG  
138  O  OD1 . ASP A 19  ? 0.0230 0.5373 0.5969 0.0131  0.0712  0.0837  19  ASP A OD1 
139  O  OD2 . ASP A 19  ? 0.4951 0.6240 0.5832 -0.0528 0.0435  0.2504  19  ASP A OD2 
140  N  N   . PHE A 20  ? 0.0273 0.2303 0.4464 -0.0633 0.0564  -0.0740 20  PHE A N   
141  C  CA  . PHE A 20  ? 0.0236 0.3002 0.5110 -0.0711 -0.0045 -0.0077 20  PHE A CA  
142  C  C   . PHE A 20  ? 0.0280 0.1433 0.4337 -0.0436 0.0022  -0.0266 20  PHE A C   
143  O  O   . PHE A 20  ? 0.0189 0.1497 0.3648 -0.0418 0.0023  -0.0461 20  PHE A O   
144  C  CB  . PHE A 20  ? 0.0115 0.4531 0.5598 -0.0034 0.0535  0.0142  20  PHE A CB  
145  C  CG  . PHE A 20  ? 0.1787 0.2764 0.5794 -0.0260 0.0261  -0.0282 20  PHE A CG  
146  C  CD1 . PHE A 20  ? 0.1534 0.3679 0.4418 0.0881  0.0030  -0.1232 20  PHE A CD1 
147  C  CD2 . PHE A 20  ? 0.2146 0.3628 0.3649 -0.0154 0.0041  -0.1551 20  PHE A CD2 
148  C  CE1 . PHE A 20  ? 0.1879 0.4291 0.5012 -0.0218 -0.0489 -0.1771 20  PHE A CE1 
149  C  CE2 . PHE A 20  ? 0.2432 0.4021 0.3421 0.0039  0.0493  -0.1161 20  PHE A CE2 
150  C  CZ  . PHE A 20  ? 0.3244 0.3775 0.3974 0.0827  -0.0557 -0.1804 20  PHE A CZ  
151  N  N   . PRO A 21  ? 0.0099 0.1864 0.4953 -0.0254 0.0046  -0.0505 21  PRO A N   
152  C  CA  . PRO A 21  ? 0.0087 0.2609 0.5069 0.0119  0.0299  -0.0162 21  PRO A CA  
153  C  C   . PRO A 21  ? 0.0117 0.2422 0.4453 -0.0354 -0.0038 0.0000  21  PRO A C   
154  O  O   . PRO A 21  ? 0.0153 0.2908 0.5170 -0.0454 -0.0296 -0.0018 21  PRO A O   
155  C  CB  . PRO A 21  ? 0.0951 0.3012 0.4773 0.0413  -0.0809 -0.0317 21  PRO A CB  
156  C  CG  . PRO A 21  ? 0.1113 0.2784 0.5285 0.0364  -0.0440 -0.0132 21  PRO A CG  
157  C  CD  . PRO A 21  ? 0.0955 0.1931 0.4526 0.0282  -0.0160 -0.1119 21  PRO A CD  
158  N  N   A ILE A 22  ? 0.0140 0.2017 0.3883 -0.0385 -0.0111 0.0222  22  ILE A N   
159  N  N   B ILE A 22  ? 0.0161 0.2290 0.4090 -0.0463 -0.0145 0.0338  22  ILE A N   
160  C  CA  A ILE A 22  ? 0.0227 0.1284 0.3345 -0.0432 -0.0035 -0.0412 22  ILE A CA  
161  C  CA  B ILE A 22  ? 0.0281 0.1555 0.3683 -0.0555 -0.0053 -0.0377 22  ILE A CA  
162  C  C   A ILE A 22  ? 0.0163 0.1619 0.3396 -0.0311 -0.0354 0.0000  22  ILE A C   
163  C  C   B ILE A 22  ? 0.0210 0.1943 0.3588 -0.0423 -0.0464 0.0177  22  ILE A C   
164  O  O   A ILE A 22  ? 0.0202 0.1290 0.2860 -0.0342 -0.0267 -0.0265 22  ILE A O   
165  O  O   B ILE A 22  ? 0.0455 0.1398 0.2917 -0.0637 -0.0315 -0.0361 22  ILE A O   
166  C  CB  A ILE A 22  ? 0.0405 0.1378 0.2800 -0.0644 -0.0259 -0.0011 22  ILE A CB  
167  C  CB  B ILE A 22  ? 0.0454 0.1835 0.3496 -0.0786 -0.0400 0.0055  22  ILE A CB  
168  C  CG1 A ILE A 22  ? 0.0249 0.1107 0.2744 -0.0415 -0.0158 -0.0180 22  ILE A CG1 
169  C  CG1 B ILE A 22  ? 0.0422 0.1326 0.3123 -0.0627 -0.0346 -0.0061 22  ILE A CG1 
170  C  CG2 A ILE A 22  ? 0.0653 0.0949 0.2362 -0.0369 -0.0060 -0.0341 22  ILE A CG2 
171  C  CG2 B ILE A 22  ? 0.0820 0.2147 0.3579 0.0128  -0.0866 -0.0514 22  ILE A CG2 
172  C  CD1 A ILE A 22  ? 0.1351 0.2079 0.2640 0.0021  -0.0581 -0.0326 22  ILE A CD1 
173  C  CD1 B ILE A 22  ? 0.0269 0.1355 0.2999 -0.0512 -0.0108 0.0062  22  ILE A CD1 
174  N  N   . ALA A 23  ? 0.0265 0.1363 0.3046 -0.0484 -0.0208 -0.0132 23  ALA A N   
175  C  CA  . ALA A 23  ? 0.0221 0.1589 0.2789 -0.0490 0.0035  -0.0074 23  ALA A CA  
176  C  C   . ALA A 23  ? 0.0236 0.1306 0.2907 -0.0456 -0.0070 -0.0124 23  ALA A C   
177  O  O   . ALA A 23  ? 0.0244 0.1400 0.2840 -0.0457 -0.0120 -0.0384 23  ALA A O   
178  C  CB  . ALA A 23  ? 0.0479 0.2359 0.4029 -0.0963 0.0045  -0.0595 23  ALA A CB  
179  N  N   . LYS A 24  ? 0.0200 0.2079 0.2895 -0.0492 -0.0199 -0.0068 24  LYS A N   
180  C  CA  . LYS A 24  ? 0.0178 0.1980 0.2807 -0.0392 -0.0333 0.0133  24  LYS A CA  
181  C  C   . LYS A 24  ? 0.0267 0.2514 0.2672 -0.0603 -0.0386 0.0028  24  LYS A C   
182  O  O   . LYS A 24  ? 0.0542 0.2400 0.3150 -0.0446 -0.0579 -0.0340 24  LYS A O   
183  C  CB  . LYS A 24  ? 0.1130 0.2943 0.3562 -0.1667 -0.0571 -0.0042 24  LYS A CB  
184  C  CG  . LYS A 24  ? 0.0604 0.3140 0.3764 -0.0436 -0.0113 0.0136  24  LYS A CG  
185  C  CD  . LYS A 24  ? 0.4355 0.8155 0.3765 -0.1889 -0.1371 -0.1170 24  LYS A CD  
186  C  CE  . LYS A 24  ? 0.4281 0.6954 0.7880 0.0956  0.0399  0.1029  24  LYS A CE  
187  N  NZ  . LYS A 24  ? 0.0372 0.5134 0.5482 -0.1157 -0.0195 -0.1229 24  LYS A NZ  
188  N  N   . GLY A 25  ? 0.0230 0.1995 0.2956 -0.0517 -0.0323 0.0153  25  GLY A N   
189  C  CA  . GLY A 25  ? 0.0644 0.2109 0.2323 -0.0414 -0.0221 -0.0039 25  GLY A CA  
190  C  C   . GLY A 25  ? 0.0527 0.2119 0.2034 -0.0269 -0.0590 0.0155  25  GLY A C   
191  O  O   . GLY A 25  ? 0.0318 0.2133 0.3080 -0.0599 -0.0524 0.0089  25  GLY A O   
192  N  N   . GLU A 26  ? 0.0432 0.2739 0.2202 -0.0432 -0.0699 0.0303  26  GLU A N   
193  C  CA  . GLU A 26  ? 0.0651 0.2330 0.1949 -0.0873 -0.0538 -0.0065 26  GLU A CA  
194  C  C   . GLU A 26  ? 0.0471 0.2290 0.1593 -0.0783 -0.0295 -0.0253 26  GLU A C   
195  O  O   . GLU A 26  ? 0.1070 0.1956 0.1738 -0.0489 -0.0348 -0.0402 26  GLU A O   
196  C  CB  . GLU A 26  ? 0.1366 0.3109 0.2805 -0.0658 -0.1357 0.0505  26  GLU A CB  
197  C  CG  . GLU A 26  ? 0.1164 0.4072 0.3531 0.0086  -0.1122 -0.0411 26  GLU A CG  
198  C  CD  . GLU A 26  ? 0.4133 0.3297 0.4572 0.0117  -0.0150 -0.0596 26  GLU A CD  
199  O  OE1 . GLU A 26  ? 0.4919 0.4005 0.6251 0.1492  -0.0820 -0.1689 26  GLU A OE1 
200  O  OE2 . GLU A 26  ? 0.4237 0.5184 0.6409 -0.0251 0.0055  -0.0035 26  GLU A OE2 
201  N  N   . ARG A 27  ? 0.0303 0.1440 0.1664 -0.0450 -0.0279 -0.0301 27  ARG A N   
202  C  CA  . ARG A 27  ? 0.0321 0.1409 0.1836 -0.0534 -0.0203 -0.0196 27  ARG A CA  
203  C  C   . ARG A 27  ? 0.0308 0.1184 0.1567 -0.0477 -0.0080 -0.0373 27  ARG A C   
204  O  O   . ARG A 27  ? 0.0297 0.1391 0.1391 -0.0511 -0.0084 -0.0335 27  ARG A O   
205  C  CB  . ARG A 27  ? 0.0372 0.1438 0.1935 -0.0624 -0.0050 -0.0366 27  ARG A CB  
206  C  CG  . ARG A 27  ? 0.0619 0.1393 0.2224 -0.0410 -0.0034 -0.0208 27  ARG A CG  
207  C  CD  . ARG A 27  ? 0.0872 0.1388 0.2044 -0.0536 -0.0091 -0.0400 27  ARG A CD  
208  N  NE  . ARG A 27  ? 0.0903 0.1478 0.1826 -0.0596 0.0173  -0.0370 27  ARG A NE  
209  C  CZ  . ARG A 27  ? 0.0119 0.1614 0.1550 -0.0279 0.0151  -0.0350 27  ARG A CZ  
210  N  NH1 . ARG A 27  ? 0.0936 0.1628 0.1460 -0.0376 0.0154  -0.0247 27  ARG A NH1 
211  N  NH2 . ARG A 27  ? 0.0457 0.1741 0.1955 -0.0390 -0.0070 -0.0365 27  ARG A NH2 
212  N  N   . GLN A 28  ? 0.0218 0.1340 0.1912 -0.0379 -0.0160 -0.0369 28  GLN A N   
213  C  CA  . GLN A 28  ? 0.0233 0.1199 0.1885 -0.0397 -0.0062 -0.0460 28  GLN A CA  
214  C  C   . GLN A 28  ? 0.0144 0.1266 0.1667 -0.0310 0.0033  -0.0231 28  GLN A C   
215  O  O   . GLN A 28  ? 0.0309 0.1506 0.1619 -0.0506 -0.0163 -0.0419 28  GLN A O   
216  C  CB  . GLN A 28  ? 0.0260 0.1287 0.2208 -0.0436 -0.0162 -0.0347 28  GLN A CB  
217  C  CG  . GLN A 28  ? 0.0230 0.1189 0.2083 -0.0426 0.0055  -0.0394 28  GLN A CG  
218  C  CD  . GLN A 28  ? 0.0125 0.0973 0.1913 -0.0130 -0.0241 -0.0249 28  GLN A CD  
219  O  OE1 . GLN A 28  ? 0.0160 0.1405 0.1956 -0.0322 -0.0138 -0.0229 28  GLN A OE1 
220  N  NE2 . GLN A 28  ? 0.0203 0.1251 0.2658 -0.0390 -0.0039 -0.0390 28  GLN A NE2 
221  N  N   . SER A 29  ? 0.0182 0.1201 0.1473 -0.0365 0.0030  -0.0230 29  SER A N   
222  C  CA  . SER A 29  ? 0.0230 0.0913 0.1429 -0.0341 -0.0103 -0.0240 29  SER A CA  
223  C  C   . SER A 29  ? 0.0240 0.0833 0.1074 -0.0354 0.0092  -0.0419 29  SER A C   
224  O  O   . SER A 29  ? 0.0177 0.1008 0.1657 -0.0321 0.0084  -0.0477 29  SER A O   
225  C  CB  . SER A 29  ? 0.0270 0.1015 0.1239 -0.0426 0.0039  -0.0366 29  SER A CB  
226  O  OG  . SER A 29  ? 0.0221 0.1048 0.1268 -0.0391 0.0074  -0.0306 29  SER A OG  
227  N  N   . PRO A 30  ? 0.0172 0.0967 0.1384 -0.0305 0.0029  -0.0329 30  PRO A N   
228  C  CA  . PRO A 30  ? 0.0192 0.1195 0.1228 -0.0381 0.0172  -0.0544 30  PRO A CA  
229  C  C   . PRO A 30  ? 0.0242 0.1118 0.1380 -0.0385 -0.0014 -0.0506 30  PRO A C   
230  O  O   . PRO A 30  ? 0.0337 0.1402 0.1608 -0.0553 -0.0114 -0.0351 30  PRO A O   
231  C  CB  . PRO A 30  ? 0.0308 0.1124 0.1342 -0.0508 0.0197  -0.0484 30  PRO A CB  
232  C  CG  . PRO A 30  ? 0.0254 0.1040 0.1563 -0.0430 0.0340  -0.0720 30  PRO A CG  
233  C  CD  . PRO A 30  ? 0.0435 0.0809 0.1365 -0.0497 0.0063  -0.0409 30  PRO A CD  
234  N  N   . VAL A 31  ? 0.0331 0.0974 0.1109 -0.0451 0.0097  -0.0551 31  VAL A N   
235  C  CA  . VAL A 31  ? 0.0408 0.1162 0.1314 -0.0521 -0.0036 -0.0563 31  VAL A CA  
236  C  C   . VAL A 31  ? 0.0330 0.1192 0.1155 -0.0497 0.0061  -0.0578 31  VAL A C   
237  O  O   . VAL A 31  ? 0.0267 0.1285 0.1261 -0.0430 0.0000  -0.0612 31  VAL A O   
238  C  CB  . VAL A 31  ? 0.0228 0.1107 0.1253 -0.0388 0.0054  -0.0512 31  VAL A CB  
239  C  CG1 . VAL A 31  ? 0.0457 0.1093 0.1443 -0.0429 0.0075  -0.0473 31  VAL A CG1 
240  C  CG2 . VAL A 31  ? 0.0409 0.1248 0.1417 -0.0639 0.0170  -0.0284 31  VAL A CG2 
241  N  N   . ASP A 32  ? 0.0324 0.1239 0.1260 -0.0467 0.0001  -0.0635 32  ASP A N   
242  C  CA  . ASP A 32  ? 0.0490 0.0943 0.1413 -0.0544 0.0042  -0.0550 32  ASP A CA  
243  C  C   . ASP A 32  ? 0.0260 0.0841 0.1104 -0.0287 -0.0041 -0.0544 32  ASP A C   
244  O  O   . ASP A 32  ? 0.0203 0.1460 0.1415 -0.0406 0.0085  -0.0290 32  ASP A O   
245  C  CB  . ASP A 32  ? 0.0621 0.1079 0.1484 -0.0583 -0.0168 -0.0568 32  ASP A CB  
246  C  CG  . ASP A 32  ? 0.0520 0.1229 0.1377 -0.0654 -0.0012 -0.0526 32  ASP A CG  
247  O  OD1 . ASP A 32  ? 0.0556 0.0982 0.1332 -0.0558 -0.0019 -0.0524 32  ASP A OD1 
248  O  OD2 . ASP A 32  ? 0.0976 0.1642 0.1474 -0.0506 -0.0011 -0.0617 32  ASP A OD2 
249  N  N   . ILE A 33  ? 0.0258 0.1163 0.1246 -0.0440 0.0065  -0.0493 33  ILE A N   
250  C  CA  . ILE A 33  ? 0.0324 0.1478 0.1592 -0.0599 0.0245  -0.0785 33  ILE A CA  
251  C  C   . ILE A 33  ? 0.0411 0.1181 0.1432 -0.0579 0.0118  -0.0428 33  ILE A C   
252  O  O   . ILE A 33  ? 0.0538 0.1251 0.1294 -0.0556 0.0138  -0.0681 33  ILE A O   
253  C  CB  . ILE A 33  ? 0.0245 0.1694 0.1523 -0.0536 0.0303  -0.0691 33  ILE A CB  
254  C  CG1 . ILE A 33  ? 0.0375 0.1821 0.1744 -0.0715 0.0187  -0.0856 33  ILE A CG1 
255  C  CG2 . ILE A 33  ? 0.0365 0.2201 0.1709 -0.0760 0.0396  -0.0502 33  ILE A CG2 
256  C  CD1 . ILE A 33  ? 0.0298 0.1668 0.1721 -0.0524 -0.0010 -0.0820 33  ILE A CD1 
257  N  N   A ASP A 34  ? 0.1143 0.0940 0.1317 -0.0741 0.0147  -0.0611 34  ASP A N   
258  N  N   B ASP A 34  ? 0.0881 0.1326 0.1329 -0.0333 0.0288  -0.0526 34  ASP A N   
259  C  CA  A ASP A 34  ? 0.0681 0.1309 0.1491 -0.0776 0.0170  -0.0822 34  ASP A CA  
260  C  CA  B ASP A 34  ? 0.1449 0.1314 0.1645 -0.0591 0.0484  -0.0668 34  ASP A CA  
261  C  C   A ASP A 34  ? 0.0985 0.1588 0.1195 -0.0823 0.0567  -0.1032 34  ASP A C   
262  C  C   B ASP A 34  ? 0.1529 0.1770 0.1568 -0.0634 0.0456  -0.0747 34  ASP A C   
263  O  O   A ASP A 34  ? 0.0890 0.1559 0.1445 -0.0839 0.0586  -0.1033 34  ASP A O   
264  O  O   B ASP A 34  ? 0.3107 0.1886 0.1690 -0.0568 0.0683  -0.0572 34  ASP A O   
265  C  CB  A ASP A 34  ? 0.1515 0.1438 0.1311 -0.1099 -0.0122 -0.0601 34  ASP A CB  
266  C  CB  B ASP A 34  ? 0.2004 0.1672 0.1623 -0.0969 0.0365  -0.0858 34  ASP A CB  
267  C  CG  A ASP A 34  ? 0.1796 0.1711 0.1412 -0.1127 0.0077  -0.0800 34  ASP A CG  
268  C  CG  B ASP A 34  ? 0.2534 0.1879 0.1982 -0.0998 0.0167  -0.1202 34  ASP A CG  
269  O  OD1 A ASP A 34  ? 0.2169 0.1395 0.2338 -0.1333 0.0478  -0.1329 34  ASP A OD1 
270  O  OD1 B ASP A 34  ? 0.2531 0.2255 0.2289 -0.1036 0.0399  -0.1586 34  ASP A OD1 
271  O  OD2 A ASP A 34  ? 0.1851 0.1706 0.1941 -0.1189 0.0601  -0.1053 34  ASP A OD2 
272  O  OD2 B ASP A 34  ? 0.2269 0.3234 0.1842 -0.0837 0.0162  -0.1273 34  ASP A OD2 
273  N  N   . THR A 35  ? 0.1259 0.1636 0.1405 -0.0748 0.0677  -0.0795 35  THR A N   
274  C  CA  . THR A 35  ? 0.1596 0.2032 0.1892 -0.1366 0.0848  -0.0794 35  THR A CA  
275  C  C   . THR A 35  ? 0.2289 0.1449 0.1929 -0.1096 0.1208  -0.0988 35  THR A C   
276  O  O   . THR A 35  ? 0.3033 0.2157 0.2694 -0.1500 0.1806  -0.0952 35  THR A O   
277  C  CB  . THR A 35  ? 0.1060 0.2304 0.2296 -0.1055 0.0584  -0.1209 35  THR A CB  
278  O  OG1 . THR A 35  ? 0.2019 0.2026 0.2260 -0.0989 0.0961  -0.0834 35  THR A OG1 
279  C  CG2 . THR A 35  ? 0.1673 0.2083 0.2080 -0.1082 0.0772  -0.1023 35  THR A CG2 
280  N  N   . HIS A 36  ? 0.2755 0.1387 0.1820 -0.1036 0.1229  -0.1120 36  HIS A N   
281  C  CA  . HIS A 36  ? 0.3239 0.2113 0.1709 -0.0994 0.0979  -0.1089 36  HIS A CA  
282  C  C   . HIS A 36  ? 0.3628 0.2353 0.1595 -0.0381 0.1129  -0.0990 36  HIS A C   
283  O  O   . HIS A 36  ? 0.2042 0.3227 0.1987 -0.1359 0.0549  -0.0810 36  HIS A O   
284  C  CB  . HIS A 36  ? 0.3991 0.2474 0.1570 -0.1279 0.0608  -0.1323 36  HIS A CB  
285  C  CG  . HIS A 36  ? 0.3162 0.2642 0.3638 -0.1597 0.1145  -0.0534 36  HIS A CG  
286  N  ND1 . HIS A 36  ? 0.5172 0.3741 0.3811 -0.0271 0.0431  0.0839  36  HIS A ND1 
287  C  CD2 . HIS A 36  ? 0.2772 0.3131 0.1901 -0.1720 -0.0074 -0.0583 36  HIS A CD2 
288  C  CE1 . HIS A 36  ? 0.7184 0.3625 0.5035 0.0244  0.0467  0.1004  36  HIS A CE1 
289  N  NE2 . HIS A 36  ? 0.7130 0.3720 0.3480 -0.0596 -0.0574 0.0019  36  HIS A NE2 
290  N  N   . THR A 37  ? 0.2272 0.1699 0.2250 -0.1073 0.0961  -0.0822 37  THR A N   
291  C  CA  . THR A 37  ? 0.2254 0.1981 0.1896 -0.1171 0.0155  -0.1177 37  THR A CA  
292  C  C   . THR A 37  ? 0.1895 0.2057 0.1583 -0.1406 0.0232  -0.0727 37  THR A C   
293  O  O   . THR A 37  ? 0.3635 0.2676 0.1754 -0.1170 0.0061  -0.0267 37  THR A O   
294  C  CB  . THR A 37  ? 0.2253 0.3041 0.3000 -0.1365 -0.0576 -0.0837 37  THR A CB  
295  O  OG1 . THR A 37  ? 0.4963 0.2382 0.3497 -0.1522 -0.0537 -0.0577 37  THR A OG1 
296  C  CG2 . THR A 37  ? 0.4505 0.2939 0.2009 -0.1277 -0.0680 -0.0998 37  THR A CG2 
297  N  N   . ALA A 38  ? 0.2102 0.2142 0.1445 -0.1292 0.0385  -0.0806 38  ALA A N   
298  C  CA  . ALA A 38  ? 0.1837 0.1873 0.1529 -0.1113 0.0412  -0.0710 38  ALA A CA  
299  C  C   . ALA A 38  ? 0.2800 0.2750 0.2267 -0.1362 0.1322  -0.1383 38  ALA A C   
300  O  O   . ALA A 38  ? 0.4132 0.2725 0.3712 -0.1134 0.2702  -0.1233 38  ALA A O   
301  C  CB  . ALA A 38  ? 0.2019 0.1957 0.1918 -0.0670 0.0055  -0.1022 38  ALA A CB  
302  N  N   . LYS A 39  ? 0.2059 0.3430 0.2222 -0.2333 0.0027  -0.0543 39  LYS A N   
303  C  CA  . LYS A 39  ? 0.3535 0.3422 0.1705 -0.2466 0.0704  -0.0870 39  LYS A CA  
304  C  C   . LYS A 39  ? 0.1859 0.2939 0.1651 -0.0840 0.0298  -0.0438 39  LYS A C   
305  O  O   . LYS A 39  ? 0.0811 0.2839 0.1767 -0.0949 0.0318  -0.0381 39  LYS A O   
306  C  CB  . LYS A 39  ? 0.3190 0.5290 0.3057 -0.2491 -0.0978 -0.0137 39  LYS A CB  
307  C  CG  . LYS A 39  ? 0.3457 0.5653 0.3141 -0.3362 -0.0855 0.0050  39  LYS A CG  
308  C  CD  . LYS A 39  ? 0.2108 0.5697 0.2280 -0.1512 -0.0597 -0.0847 39  LYS A CD  
309  C  CE  . LYS A 39  ? 0.4776 0.3910 0.3209 -0.1082 0.0846  -0.0963 39  LYS A CE  
310  N  NZ  . LYS A 39  ? 0.3691 0.5466 0.4486 0.0429  0.1364  -0.2426 39  LYS A NZ  
311  N  N   . TYR A 40  ? 0.2183 0.2720 0.2540 -0.0886 0.0558  -0.0712 40  TYR A N   
312  C  CA  . TYR A 40  ? 0.1408 0.2278 0.2224 -0.0212 0.0708  -0.0365 40  TYR A CA  
313  C  C   . TYR A 40  ? 0.1302 0.2365 0.2021 -0.0219 0.0254  -0.0488 40  TYR A C   
314  O  O   . TYR A 40  ? 0.1395 0.2667 0.1913 -0.1064 0.0611  -0.0445 40  TYR A O   
315  C  CB  . TYR A 40  ? 0.1603 0.3585 0.1984 0.0067  0.0886  -0.0705 40  TYR A CB  
316  C  CG  . TYR A 40  ? 0.2031 0.4044 0.2463 -0.0092 0.0961  -0.0047 40  TYR A CG  
317  C  CD1 . TYR A 40  ? 0.1779 0.4038 0.2696 0.0181  0.0252  -0.0050 40  TYR A CD1 
318  C  CD2 . TYR A 40  ? 0.3161 0.5368 0.1952 0.1076  0.1312  -0.0225 40  TYR A CD2 
319  C  CE1 . TYR A 40  ? 0.1544 0.5623 0.3085 -0.0130 0.0433  -0.0839 40  TYR A CE1 
320  C  CE2 . TYR A 40  ? 0.3380 0.7020 0.3134 0.0082  0.0939  -0.0425 40  TYR A CE2 
321  C  CZ  . TYR A 40  ? 0.2320 0.6919 0.2377 0.1287  0.0359  0.0391  40  TYR A CZ  
322  O  OH  . TYR A 40  ? 0.2896 0.7510 0.4139 0.0354  -0.0946 0.0053  40  TYR A OH  
323  N  N   . ASP A 41  ? 0.0696 0.2254 0.1940 -0.0546 0.0580  -0.0422 41  ASP A N   
324  C  CA  . ASP A 41  ? 0.0362 0.2485 0.2529 -0.0333 0.0127  0.0092  41  ASP A CA  
325  C  C   . ASP A 41  ? 0.0180 0.3221 0.2525 -0.0306 0.0471  -0.0100 41  ASP A C   
326  O  O   . ASP A 41  ? 0.0976 0.3820 0.2294 -0.0895 0.0586  -0.0236 41  ASP A O   
327  C  CB  . ASP A 41  ? 0.0420 0.2251 0.4021 -0.0274 -0.0369 -0.0154 41  ASP A CB  
328  C  CG  . ASP A 41  ? 0.1415 0.2546 0.4323 -0.0335 -0.0454 0.0267  41  ASP A CG  
329  O  OD1 . ASP A 41  ? 0.3150 0.3069 0.2997 -0.1302 0.0142  0.0120  41  ASP A OD1 
330  O  OD2 . ASP A 41  ? 0.1200 0.3153 0.4170 -0.0339 -0.0851 0.0216  41  ASP A OD2 
331  N  N   . PRO A 42  ? 0.1033 0.4349 0.2518 -0.1122 0.0857  -0.0400 42  PRO A N   
332  C  CA  . PRO A 42  ? 0.1226 0.4782 0.3666 -0.1771 0.1338  -0.1439 42  PRO A CA  
333  C  C   . PRO A 42  ? 0.2058 0.4353 0.3585 -0.0762 0.1036  -0.0576 42  PRO A C   
334  O  O   . PRO A 42  ? 0.1778 0.5817 0.4688 -0.0323 0.0644  -0.0278 42  PRO A O   
335  C  CB  . PRO A 42  ? 0.0849 0.6666 0.4220 -0.1903 0.1201  -0.0762 42  PRO A CB  
336  C  CG  . PRO A 42  ? 0.1207 0.7013 0.3937 -0.2575 0.0850  0.0012  42  PRO A CG  
337  C  CD  . PRO A 42  ? 0.1044 0.6170 0.2511 -0.1779 0.1233  -0.0632 42  PRO A CD  
338  N  N   . SER A 43  ? 0.1929 0.3253 0.3227 -0.1206 0.0794  -0.0089 43  SER A N   
339  C  CA  . SER A 43  ? 0.4566 0.2734 0.2707 -0.1720 0.0079  0.0209  43  SER A CA  
340  C  C   . SER A 43  ? 0.2911 0.3567 0.3041 -0.2243 -0.0138 -0.0590 43  SER A C   
341  O  O   . SER A 43  ? 0.4770 0.3624 0.3551 -0.2165 -0.1052 -0.0395 43  SER A O   
342  C  CB  . SER A 43  ? 0.2685 0.2962 0.4895 -0.1996 -0.0187 0.0346  43  SER A CB  
343  O  OG  . SER A 43  ? 0.2929 0.4134 0.3892 -0.1411 -0.0431 0.0001  43  SER A OG  
344  N  N   . LEU A 44  ? 0.2383 0.3649 0.3295 -0.2208 0.0082  -0.0714 44  LEU A N   
345  C  CA  . LEU A 44  ? 0.1537 0.4911 0.3642 -0.1627 -0.0403 -0.1136 44  LEU A CA  
346  C  C   . LEU A 44  ? 0.1394 0.4023 0.3856 -0.0844 -0.0190 -0.1761 44  LEU A C   
347  O  O   . LEU A 44  ? 0.1856 0.6759 0.3802 0.0062  0.0557  -0.1811 44  LEU A O   
348  C  CB  . LEU A 44  ? 0.1069 0.3779 0.2911 -0.0579 -0.0264 -0.1206 44  LEU A CB  
349  C  CG  . LEU A 44  ? 0.0708 0.2981 0.2771 -0.0471 0.0280  -0.0624 44  LEU A CG  
350  C  CD1 . LEU A 44  ? 0.1389 0.2534 0.2350 0.0386  0.0367  -0.0574 44  LEU A CD1 
351  C  CD2 . LEU A 44  ? 0.1167 0.2223 0.2768 -0.0409 -0.0190 -0.0346 44  LEU A CD2 
352  N  N   . LYS A 45  ? 0.1635 0.5017 0.3121 -0.0930 -0.0184 -0.1673 45  LYS A N   
353  C  CA  . LYS A 45  ? 0.1481 0.3854 0.3759 -0.0576 -0.0683 -0.0499 45  LYS A CA  
354  C  C   . LYS A 45  ? 0.1032 0.5255 0.2969 -0.1121 0.0414  -0.0344 45  LYS A C   
355  O  O   . LYS A 45  ? 0.0883 0.4110 0.3388 -0.0446 0.0262  0.0066  45  LYS A O   
356  C  CB  . LYS A 45  ? 0.2324 0.4056 0.3341 -0.1045 -0.0416 -0.0924 45  LYS A CB  
357  C  CG  . LYS A 45  ? 0.1876 0.6057 0.4004 0.0095  -0.0107 0.0385  45  LYS A CG  
358  C  CD  . LYS A 45  ? 0.2919 0.5992 0.7668 -0.0779 -0.0127 -0.0640 45  LYS A CD  
359  C  CE  . LYS A 45  ? 0.7702 0.7643 0.8097 -0.0683 0.0663  0.2813  45  LYS A CE  
360  N  NZ  . LYS A 45  ? 0.3902 1.3704 1.1241 -0.3461 0.3337  0.2597  45  LYS A NZ  
361  N  N   . PRO A 46  ? 0.1125 0.5101 0.3653 0.0607  0.0694  -0.0554 46  PRO A N   
362  C  CA  . PRO A 46  ? 0.0568 0.4611 0.3292 0.0105  0.0450  -0.1062 46  PRO A CA  
363  C  C   . PRO A 46  ? 0.2058 0.3802 0.2481 0.0690  0.0519  -0.0013 46  PRO A C   
364  O  O   . PRO A 46  ? 0.2234 0.3547 0.2800 0.0390  0.0149  -0.1247 46  PRO A O   
365  C  CB  . PRO A 46  ? 0.0691 0.4158 0.4068 -0.0892 0.1013  -0.0195 46  PRO A CB  
366  C  CG  . PRO A 46  ? 0.2201 1.8652 1.3083 -0.3389 0.4709  -0.1553 46  PRO A CG  
367  C  CD  . PRO A 46  ? 0.2824 0.6071 0.4305 -0.2460 0.1219  -0.0580 46  PRO A CD  
368  N  N   . LEU A 47  ? 0.1091 0.5049 0.4502 -0.1527 0.0864  -0.0276 47  LEU A N   
369  C  CA  . LEU A 47  ? 0.0211 0.2183 0.3882 -0.0088 0.0361  -0.0348 47  LEU A CA  
370  C  C   . LEU A 47  ? 0.0081 0.3593 0.4854 -0.0253 0.0073  -0.0603 47  LEU A C   
371  O  O   . LEU A 47  ? 0.0374 0.3472 0.4874 0.0247  -0.0734 -0.1300 47  LEU A O   
372  C  CB  . LEU A 47  ? 0.2520 0.4081 0.3569 -0.1531 0.0436  0.0379  47  LEU A CB  
373  C  CG  . LEU A 47  ? 0.1625 0.3683 0.4176 0.0468  -0.0334 0.1590  47  LEU A CG  
374  C  CD1 . LEU A 47  ? 0.2536 0.4300 0.5373 0.1339  -0.0856 0.0193  47  LEU A CD1 
375  C  CD2 . LEU A 47  ? 1.1296 2.4419 1.9985 -0.9994 0.6147  0.1323  47  LEU A CD2 
376  N  N   . SER A 48  ? 0.0101 0.3089 0.4433 -0.0119 -0.0362 -0.0433 48  SER A N   
377  C  CA  . SER A 48  ? 0.0107 0.2035 0.3235 -0.0245 -0.0168 -0.0333 48  SER A CA  
378  C  C   . SER A 48  ? 0.0227 0.2170 0.3031 -0.0375 -0.0074 -0.0612 48  SER A C   
379  O  O   . SER A 48  ? 0.0221 0.2188 0.2701 -0.0070 0.0122  -0.0295 48  SER A O   
380  C  CB  . SER A 48  ? 0.0190 0.2021 0.3723 -0.0361 0.0319  -0.0454 48  SER A CB  
381  O  OG  . SER A 48  ? 0.1086 0.2960 0.4734 -0.1128 0.0083  -0.0945 48  SER A OG  
382  N  N   . VAL A 49  ? 0.0429 0.2383 0.2935 -0.0141 -0.0210 -0.0591 49  VAL A N   
383  C  CA  . VAL A 49  ? 0.1010 0.2741 0.3264 0.0359  0.0055  -0.0063 49  VAL A CA  
384  C  C   . VAL A 49  ? 0.1053 0.2412 0.3459 0.0375  -0.0032 -0.0078 49  VAL A C   
385  O  O   . VAL A 49  ? 0.1372 0.4176 0.3486 0.1276  -0.0329 -0.0768 49  VAL A O   
386  C  CB  . VAL A 49  ? 0.0820 0.2956 0.5072 0.0201  0.0684  0.0230  49  VAL A CB  
387  C  CG1 . VAL A 49  ? 0.2506 0.3159 0.4524 0.1327  0.0625  0.0058  49  VAL A CG1 
388  C  CG2 . VAL A 49  ? 0.0644 0.2144 0.5299 -0.0575 0.0795  0.0408  49  VAL A CG2 
389  N  N   . SER A 50  ? 0.1658 0.2335 0.2991 0.0111  -0.0392 -0.0177 50  SER A N   
390  C  CA  . SER A 50  ? 0.1106 0.2512 0.4400 -0.0080 -0.0543 -0.0143 50  SER A CA  
391  C  C   . SER A 50  ? 0.1450 0.2830 0.3906 -0.0281 -0.0800 -0.0234 50  SER A C   
392  O  O   . SER A 50  ? 0.1215 0.2312 0.3702 -0.0527 -0.0664 -0.0463 50  SER A O   
393  C  CB  . SER A 50  ? 0.1854 0.2642 0.5105 -0.1207 -0.1110 -0.0474 50  SER A CB  
394  O  OG  . SER A 50  ? 0.2486 0.4037 0.7984 -0.0810 0.0418  0.1381  50  SER A OG  
395  N  N   . TYR A 51  ? 0.1743 0.2640 0.5216 -0.0148 -0.0988 0.0217  51  TYR A N   
396  C  CA  . TYR A 51  ? 0.1813 0.2376 0.4639 -0.0165 -0.1165 -0.0579 51  TYR A CA  
397  C  C   . TYR A 51  ? 0.1674 0.2947 0.4072 -0.0359 -0.1313 -0.0653 51  TYR A C   
398  O  O   . TYR A 51  ? 0.1835 0.2618 0.3541 -0.0381 -0.1028 -0.0899 51  TYR A O   
399  C  CB  . TYR A 51  ? 0.0824 0.2283 0.3747 -0.0390 -0.1201 -0.0434 51  TYR A CB  
400  C  CG  . TYR A 51  ? 0.0660 0.2139 0.3093 -0.0369 -0.0892 -0.0239 51  TYR A CG  
401  C  CD1 . TYR A 51  ? 0.0553 0.2106 0.2956 -0.0384 -0.0446 0.0035  51  TYR A CD1 
402  C  CD2 . TYR A 51  ? 0.0807 0.2028 0.2606 -0.0398 -0.0577 -0.0812 51  TYR A CD2 
403  C  CE1 . TYR A 51  ? 0.0938 0.1550 0.2485 -0.0150 -0.0594 -0.0513 51  TYR A CE1 
404  C  CE2 . TYR A 51  ? 0.0518 0.1777 0.2309 -0.0006 -0.0438 -0.0790 51  TYR A CE2 
405  C  CZ  . TYR A 51  ? 0.0666 0.1490 0.2597 -0.0273 -0.0531 -0.0514 51  TYR A CZ  
406  O  OH  . TYR A 51  ? 0.0690 0.1858 0.2291 -0.0425 -0.0475 -0.0244 51  TYR A OH  
407  N  N   . ASP A 52  ? 0.2175 0.3065 0.7134 0.0206  -0.1056 -0.0707 52  ASP A N   
408  C  CA  . ASP A 52  ? 0.1570 0.4967 0.4820 -0.0441 -0.1120 -0.0762 52  ASP A CA  
409  C  C   . ASP A 52  ? 0.1881 0.4076 0.4887 -0.0013 -0.0337 -0.0449 52  ASP A C   
410  O  O   . ASP A 52  ? 0.3722 0.5248 0.4474 0.1367  -0.1153 -0.1768 52  ASP A O   
411  C  CB  . ASP A 52  ? 0.2231 0.7202 0.7160 -0.1922 -0.1581 -0.1583 52  ASP A CB  
412  C  CG  . ASP A 52  ? 0.3809 0.7578 0.7798 0.2219  -0.0264 -0.0534 52  ASP A CG  
413  O  OD1 . ASP A 52  ? 0.3924 1.0542 0.7371 0.2054  0.1365  0.1264  52  ASP A OD1 
414  O  OD2 . ASP A 52  ? 0.5771 1.5648 1.0319 -0.3484 -0.1057 -0.4332 52  ASP A OD2 
415  N  N   . GLN A 53  ? 0.1817 0.3035 0.6000 0.0016  -0.1014 -0.1571 53  GLN A N   
416  C  CA  . GLN A 53  ? 0.1588 0.4242 0.5950 0.0965  -0.0832 -0.1597 53  GLN A CA  
417  C  C   . GLN A 53  ? 0.2074 0.1999 0.4834 -0.0194 -0.1011 -0.0646 53  GLN A C   
418  O  O   . GLN A 53  ? 0.3069 0.1842 0.5247 -0.0186 -0.1434 -0.1168 53  GLN A O   
419  C  CB  . GLN A 53  ? 0.5170 0.5806 0.9484 0.1403  -0.0905 -0.0472 53  GLN A CB  
420  C  CG  . GLN A 53  ? 0.5181 0.7420 0.7219 0.1557  0.0110  -0.2640 53  GLN A CG  
421  C  CD  . GLN A 53  ? 0.9095 1.0618 0.7062 0.3400  -0.1317 0.0521  53  GLN A CD  
422  O  OE1 . GLN A 53  ? 0.8051 1.4060 0.8827 -0.2938 -0.0322 -0.0364 53  GLN A OE1 
423  N  NE2 . GLN A 53  ? 1.0027 1.1637 0.5580 0.3464  -0.0160 -0.1932 53  GLN A NE2 
424  N  N   . ALA A 54  ? 0.3075 0.1856 0.4695 -0.0125 -0.1462 -0.0937 54  ALA A N   
425  C  CA  . ALA A 54  ? 0.3129 0.1760 0.3073 -0.0207 -0.1406 -0.0291 54  ALA A CA  
426  C  C   . ALA A 54  ? 0.3287 0.1794 0.3017 -0.0051 -0.1326 -0.0241 54  ALA A C   
427  O  O   . ALA A 54  ? 0.3268 0.2019 0.3397 0.0052  -0.1615 -0.0493 54  ALA A O   
428  C  CB  . ALA A 54  ? 0.3109 0.1579 0.3702 -0.0427 -0.0960 -0.0244 54  ALA A CB  
429  N  N   . THR A 55  ? 0.2378 0.1772 0.2966 -0.0480 -0.1516 -0.0438 55  THR A N   
430  C  CA  . THR A 55  ? 0.2385 0.1583 0.3048 0.0157  -0.1681 -0.1036 55  THR A CA  
431  C  C   . THR A 55  ? 0.3533 0.1372 0.2257 -0.0618 -0.1492 -0.0785 55  THR A C   
432  O  O   . THR A 55  ? 0.4073 0.1179 0.2509 -0.0479 -0.1108 -0.0871 55  THR A O   
433  C  CB  . THR A 55  ? 0.4308 0.1646 0.4198 0.0008  -0.1223 -0.1313 55  THR A CB  
434  O  OG1 . THR A 55  ? 0.4954 0.2101 0.3003 -0.0567 -0.0904 -0.0838 55  THR A OG1 
435  C  CG2 . THR A 55  ? 0.5370 0.2124 0.3860 -0.0820 -0.0862 -0.0320 55  THR A CG2 
436  N  N   . SER A 56  ? 0.4836 0.1524 0.2570 -0.0231 -0.1699 -0.0525 56  SER A N   
437  C  CA  . SER A 56  ? 0.4394 0.1810 0.2420 0.0475  -0.1583 -0.0553 56  SER A CA  
438  C  C   . SER A 56  ? 0.4821 0.2061 0.2550 -0.0377 -0.1157 -0.0528 56  SER A C   
439  O  O   . SER A 56  ? 0.6354 0.1848 0.2867 -0.0348 -0.1585 -0.0046 56  SER A O   
440  C  CB  . SER A 56  ? 0.5568 0.1883 0.2676 0.0303  -0.2279 -0.0298 56  SER A CB  
441  O  OG  . SER A 56  ? 0.4838 0.1578 0.2688 -0.0081 -0.2236 -0.0797 56  SER A OG  
442  N  N   A LEU A 57  ? 0.4551 0.1555 0.1782 -0.0392 -0.0343 -0.0400 57  LEU A N   
443  N  N   B LEU A 57  ? 0.4767 0.1588 0.2032 -0.0241 -0.0431 -0.0326 57  LEU A N   
444  C  CA  A LEU A 57  ? 0.3301 0.1836 0.1899 -0.1163 0.0131  -0.0537 57  LEU A CA  
445  C  CA  B LEU A 57  ? 0.4635 0.2622 0.2300 -0.0357 -0.0491 -0.1178 57  LEU A CA  
446  C  C   A LEU A 57  ? 0.0591 0.3794 0.2090 -0.1391 0.0644  -0.1400 57  LEU A C   
447  C  C   B LEU A 57  ? 0.3365 0.3033 0.2098 -0.0200 0.0132  -0.1650 57  LEU A C   
448  O  O   A LEU A 57  ? 0.1043 0.1670 0.1889 -0.0950 -0.0226 -0.0881 57  LEU A O   
449  O  O   B LEU A 57  ? 0.2370 0.2833 0.2545 -0.0177 0.0128  -0.0891 57  LEU A O   
450  C  CB  A LEU A 57  ? 0.5364 0.0949 0.1953 -0.0810 -0.1337 -0.0882 57  LEU A CB  
451  C  CB  B LEU A 57  ? 0.5593 0.2833 0.2858 0.0568  -0.0634 -0.1382 57  LEU A CB  
452  C  CG  A LEU A 57  ? 0.5603 0.1567 0.2051 -0.1620 -0.1467 -0.0854 57  LEU A CG  
453  C  CG  B LEU A 57  ? 0.4692 0.2281 0.4745 -0.0223 -0.0436 -0.1032 57  LEU A CG  
454  C  CD1 A LEU A 57  ? 0.6187 0.1700 0.3924 -0.0741 -0.0554 -0.1253 57  LEU A CD1 
455  C  CD1 B LEU A 57  ? 0.6963 0.1773 0.4103 -0.0694 0.2258  -0.0873 57  LEU A CD1 
456  C  CD2 A LEU A 57  ? 0.4528 0.1503 0.3470 -0.1314 -0.0627 -0.0363 57  LEU A CD2 
457  C  CD2 B LEU A 57  ? 0.4226 0.2074 0.4311 -0.1048 0.0068  -0.0354 57  LEU A CD2 
458  N  N   A ARG A 58  ? 0.0791 0.3010 0.3999 -0.1395 -0.0190 -0.0669 58  ARG A N   
459  N  N   B ARG A 58  ? 0.2800 0.2795 0.1679 -0.0849 -0.0587 -0.1157 58  ARG A N   
460  C  CA  A ARG A 58  ? 0.0431 0.2861 0.2461 -0.0962 0.0828  -0.1785 58  ARG A CA  
461  C  CA  B ARG A 58  ? 0.1922 0.2943 0.2057 -0.0289 -0.0842 -0.1839 58  ARG A CA  
462  C  C   A ARG A 58  ? 0.0257 0.1611 0.1530 -0.0523 0.0362  -0.0831 58  ARG A C   
463  C  C   B ARG A 58  ? 0.3321 0.1357 0.1295 -0.0308 0.0148  -0.0783 58  ARG A C   
464  O  O   A ARG A 58  ? 0.0291 0.2131 0.1598 -0.0681 0.0117  -0.0547 58  ARG A O   
465  O  O   B ARG A 58  ? 0.3322 0.1321 0.1258 -0.0737 0.0337  -0.0684 58  ARG A O   
466  C  CB  A ARG A 58  ? 0.0231 0.4081 0.2646 -0.0389 0.0655  -0.1774 58  ARG A CB  
467  C  CB  B ARG A 58  ? 0.1491 0.4879 0.1417 0.0646  0.0295  -0.1122 58  ARG A CB  
468  C  CG  A ARG A 58  ? 0.0518 0.1420 0.2395 -0.0434 0.0675  -0.1763 58  ARG A CG  
469  C  CG  B ARG A 58  ? 0.0863 0.6626 0.4336 0.2132  0.0749  0.0229  58  ARG A CG  
470  C  CD  A ARG A 58  ? 0.0705 0.1906 0.1984 0.0308  -0.0113 -0.1222 58  ARG A CD  
471  C  CD  B ARG A 58  ? 0.0623 0.3758 0.2516 0.0035  0.0804  -0.0164 58  ARG A CD  
472  N  NE  A ARG A 58  ? 0.0216 0.1461 0.2123 -0.0435 0.0065  -0.0753 58  ARG A NE  
473  N  NE  B ARG A 58  ? 0.0445 0.2164 0.3526 -0.0865 0.0424  -0.0327 58  ARG A NE  
474  C  CZ  A ARG A 58  ? 0.0074 0.2269 0.1700 -0.0108 0.0133  -0.1244 58  ARG A CZ  
475  C  CZ  B ARG A 58  ? 0.0254 0.1470 0.3077 -0.0293 0.0209  -0.1418 58  ARG A CZ  
476  N  NH1 A ARG A 58  ? 0.1018 0.1227 0.1644 -0.0392 0.0665  -0.0647 58  ARG A NH1 
477  N  NH1 B ARG A 58  ? 0.0300 0.2952 0.3295 -0.0542 0.0089  -0.1294 58  ARG A NH1 
478  N  NH2 A ARG A 58  ? 0.0490 0.1400 0.1691 0.0084  -0.0016 -0.0585 58  ARG A NH2 
479  N  NH2 B ARG A 58  ? 0.2296 0.2953 0.3250 -0.1630 0.0974  -0.0897 58  ARG A NH2 
480  N  N   A ILE A 59  ? 0.0221 0.1227 0.1565 -0.0428 0.0370  -0.0974 59  ILE A N   
481  N  N   B ILE A 59  ? 0.3360 0.1673 0.0852 0.0133  0.0722  -0.0977 59  ILE A N   
482  C  CA  A ILE A 59  ? 0.0261 0.1375 0.2053 -0.0476 0.0171  -0.0963 59  ILE A CA  
483  C  CA  B ILE A 59  ? 0.3459 0.1953 0.0676 -0.0154 0.0244  -0.0672 59  ILE A CA  
484  C  C   A ILE A 59  ? 0.0778 0.1521 0.3009 -0.0960 0.0118  -0.0857 59  ILE A C   
485  C  C   B ILE A 59  ? 0.3493 0.1012 0.1128 -0.0318 -0.0271 -0.0954 59  ILE A C   
486  O  O   A ILE A 59  ? 0.3476 1.9423 0.4395 -0.8123 0.1589  -0.3494 59  ILE A O   
487  O  O   B ILE A 59  ? 0.4798 0.0915 0.0897 -0.0019 -0.0204 -0.0838 59  ILE A O   
488  C  CB  A ILE A 59  ? 0.0297 0.1444 0.1780 -0.0509 0.0557  -0.0891 59  ILE A CB  
489  C  CB  B ILE A 59  ? 0.2165 0.1755 0.1188 -0.0139 -0.0059 -0.0999 59  ILE A CB  
490  C  CG1 A ILE A 59  ? 0.0456 0.1507 0.1608 -0.0504 0.0368  -0.0978 59  ILE A CG1 
491  C  CG1 B ILE A 59  ? 0.0378 0.1657 0.1471 -0.0472 -0.0222 -0.0263 59  ILE A CG1 
492  C  CG2 A ILE A 59  ? 0.0125 0.2339 0.1689 -0.0254 -0.0064 -0.1117 59  ILE A CG2 
493  C  CG2 B ILE A 59  ? 0.0141 0.2385 0.1430 -0.0235 -0.0203 -0.0544 59  ILE A CG2 
494  C  CD1 A ILE A 59  ? 0.0843 0.1040 0.1265 -0.0736 0.0005  -0.0571 59  ILE A CD1 
495  C  CD1 B ILE A 59  ? 0.0370 0.1683 0.2132 -0.0320 -0.0362 -0.1070 59  ILE A CD1 
496  N  N   A LEU A 60  ? 0.0572 0.2358 0.3001 -0.0950 -0.0161 -0.0918 60  LEU A N   
497  N  N   B LEU A 60  ? 0.1538 0.2944 0.1877 -0.0444 -0.0255 -0.0489 60  LEU A N   
498  C  CA  A LEU A 60  ? 0.0326 0.1800 0.1085 -0.0532 -0.0024 -0.0766 60  LEU A CA  
499  C  CA  B LEU A 60  ? 0.2033 0.0913 0.2900 -0.1100 -0.0405 -0.0185 60  LEU A CA  
500  C  C   A LEU A 60  ? 0.1894 0.1459 0.1447 -0.0600 -0.0666 -0.0951 60  LEU A C   
501  C  C   B LEU A 60  ? 0.4724 1.0484 1.2533 -0.6969 0.0520  -0.0780 60  LEU A C   
502  O  O   A LEU A 60  ? 0.2940 0.1173 0.0766 0.0086  0.0047  -0.0611 60  LEU A O   
503  O  O   B LEU A 60  ? 0.3545 1.0969 1.3276 -0.6136 0.0834  -0.0399 60  LEU A O   
504  C  CB  A LEU A 60  ? 0.0774 0.2579 0.2494 -0.1336 0.0386  -0.0809 60  LEU A CB  
505  C  CB  B LEU A 60  ? 0.4350 0.0899 0.2768 -0.0033 -0.0688 -0.0331 60  LEU A CB  
506  C  CG  A LEU A 60  ? 0.1901 0.4731 0.2737 -0.2908 0.1031  -0.2002 60  LEU A CG  
507  C  CG  B LEU A 60  ? 0.4585 0.0579 0.1034 0.0258  -0.0452 -0.0672 60  LEU A CG  
508  C  CD1 A LEU A 60  ? 0.1185 0.2492 0.2406 -0.0044 0.0644  -0.0638 60  LEU A CD1 
509  C  CD1 B LEU A 60  ? 0.4617 0.1039 0.1274 0.0480  -0.0087 -0.0710 60  LEU A CD1 
510  C  CD2 A LEU A 60  ? 0.0815 0.4722 0.3660 -0.0352 0.1071  -0.1627 60  LEU A CD2 
511  C  CD2 B LEU A 60  ? 0.5419 0.0890 0.1371 0.0271  -0.0882 -0.0429 60  LEU A CD2 
512  N  N   A ASN A 61  ? 0.3010 0.1217 0.0996 0.0350  0.0174  -0.0992 61  ASN A N   
513  N  N   B ASN A 61  ? 0.0280 0.1584 0.9347 -0.0498 0.0598  0.0317  61  ASN A N   
514  C  CA  A ASN A 61  ? 0.3055 0.0895 0.0949 0.0603  0.0296  -0.0452 61  ASN A CA  
515  C  CA  B ASN A 61  ? 0.0671 0.1941 0.4536 -0.1068 0.0111  -0.0174 61  ASN A CA  
516  C  C   A ASN A 61  ? 0.3639 0.0946 0.1490 0.0988  0.0017  -0.0796 61  ASN A C   
517  C  C   B ASN A 61  ? 0.0209 0.2536 0.2521 0.0027  -0.0488 -0.1181 61  ASN A C   
518  O  O   A ASN A 61  ? 0.3492 0.1175 0.1328 0.0601  0.0030  -0.0394 61  ASN A O   
519  O  O   B ASN A 61  ? 0.0184 0.1394 0.3354 -0.0375 0.0209  -0.1333 61  ASN A O   
520  C  CB  A ASN A 61  ? 0.2828 0.1319 0.1507 0.0253  0.0839  -0.0499 61  ASN A CB  
521  C  CB  B ASN A 61  ? 0.0785 0.1829 0.2548 -0.0722 0.0093  -0.0551 61  ASN A CB  
522  C  CG  A ASN A 61  ? 0.2813 0.1039 0.1195 0.0824  0.0308  -0.0724 61  ASN A CG  
523  C  CG  B ASN A 61  ? 0.0147 0.1714 0.1863 -0.0254 -0.0252 -0.0189 61  ASN A CG  
524  O  OD1 A ASN A 61  ? 0.3203 0.0901 0.0930 0.0925  0.0384  -0.0511 61  ASN A OD1 
525  O  OD1 B ASN A 61  ? 0.1579 0.6569 0.7154 -0.2265 -0.0765 -0.3430 61  ASN A OD1 
526  N  ND2 A ASN A 61  ? 0.2500 0.1010 0.1016 0.0345  0.0271  -0.0789 61  ASN A ND2 
527  N  ND2 B ASN A 61  ? 0.1015 0.2326 0.1897 0.0131  0.0282  -0.0006 61  ASN A ND2 
528  N  N   . ASN A 62  ? 0.3207 0.1581 0.1597 0.0705  -0.0168 -0.0660 62  ASN A N   
529  C  CA  . ASN A 62  ? 0.3752 0.2199 0.2264 0.1339  0.0038  -0.0402 62  ASN A CA  
530  C  C   . ASN A 62  ? 0.3359 0.2567 0.1289 0.1525  0.0499  -0.0540 62  ASN A C   
531  O  O   . ASN A 62  ? 0.4607 0.2753 0.1852 0.2143  0.0070  -0.0590 62  ASN A O   
532  C  CB  . ASN A 62  ? 0.4686 0.1631 0.1849 0.0746  -0.0340 -0.0561 62  ASN A CB  
533  C  CG  . ASN A 62  ? 0.3762 0.1707 0.1910 0.0881  -0.0312 -0.0491 62  ASN A CG  
534  O  OD1 . ASN A 62  ? 0.2667 0.1703 0.1671 0.0670  0.0291  -0.0355 62  ASN A OD1 
535  N  ND2 . ASN A 62  ? 0.3028 0.2086 0.1987 -0.0065 -0.0530 -0.0894 62  ASN A ND2 
536  N  N   . GLY A 63  ? 0.3609 0.2656 0.1745 0.1201  0.0621  -0.0641 63  GLY A N   
537  C  CA  . GLY A 63  ? 0.2680 0.2535 0.1776 0.1712  0.0441  -0.0621 63  GLY A CA  
538  C  C   . GLY A 63  ? 0.2918 0.1779 0.2077 0.0737  0.0903  -0.0238 63  GLY A C   
539  O  O   . GLY A 63  ? 0.1700 0.2693 0.1866 0.0624  0.0996  -0.0256 63  GLY A O   
540  N  N   . HIS A 64  ? 0.1934 0.1806 0.1434 0.0583  0.0249  -0.0485 64  HIS A N   
541  C  CA  . HIS A 64  ? 0.1485 0.2344 0.1473 0.0753  0.0491  -0.0684 64  HIS A CA  
542  C  C   . HIS A 64  ? 0.1588 0.2079 0.1158 0.0754  0.0066  -0.0657 64  HIS A C   
543  O  O   . HIS A 64  ? 0.1768 0.1920 0.1611 0.0604  0.0227  -0.0636 64  HIS A O   
544  C  CB  . HIS A 64  ? 0.1759 0.2087 0.1542 0.0753  0.0381  -0.0548 64  HIS A CB  
545  C  CG  . HIS A 64  ? 0.1459 0.2544 0.1594 0.0568  0.0706  -0.0290 64  HIS A CG  
546  N  ND1 . HIS A 64  ? 0.1317 0.3533 0.2439 0.0501  0.0947  0.0421  64  HIS A ND1 
547  C  CD2 . HIS A 64  ? 0.2075 0.2490 0.1988 0.0722  0.0316  -0.0190 64  HIS A CD2 
548  C  CE1 . HIS A 64  ? 0.1914 0.3673 0.2345 0.0715  0.1080  0.0080  64  HIS A CE1 
549  N  NE2 . HIS A 64  ? 0.2382 0.3217 0.2825 0.1285  0.0832  0.0222  64  HIS A NE2 
550  N  N   . SER A 65  ? 0.1682 0.1909 0.1356 0.0491  0.0006  -0.0712 65  SER A N   
551  C  CA  . SER A 65  ? 0.1439 0.1256 0.1449 0.0261  0.0334  -0.0732 65  SER A CA  
552  C  C   . SER A 65  ? 0.2116 0.0894 0.1254 0.0250  0.0166  -0.0568 65  SER A C   
553  O  O   . SER A 65  ? 0.2214 0.1844 0.1419 0.0476  0.0324  -0.0593 65  SER A O   
554  C  CB  . SER A 65  ? 0.1597 0.1606 0.1311 0.0247  0.0163  -0.0612 65  SER A CB  
555  O  OG  . SER A 65  ? 0.1575 0.1979 0.1717 0.0201  -0.0402 -0.0899 65  SER A OG  
556  N  N   . PHE A 66  ? 0.1913 0.0928 0.1668 -0.0030 -0.0120 -0.0643 66  PHE A N   
557  C  CA  . PHE A 66  ? 0.2552 0.1215 0.1405 -0.0172 -0.0335 -0.0693 66  PHE A CA  
558  C  C   . PHE A 66  ? 0.2674 0.1046 0.1227 -0.0396 -0.0547 -0.0629 66  PHE A C   
559  O  O   . PHE A 66  ? 0.2138 0.1059 0.1297 -0.0261 -0.0160 -0.0537 66  PHE A O   
560  C  CB  . PHE A 66  ? 0.2018 0.1484 0.1473 -0.0278 -0.0236 -0.0449 66  PHE A CB  
561  C  CG  . PHE A 66  ? 0.2496 0.1400 0.1247 -0.0131 -0.0196 -0.0440 66  PHE A CG  
562  C  CD1 . PHE A 66  ? 0.2685 0.1476 0.1355 -0.0424 -0.0167 -0.0212 66  PHE A CD1 
563  C  CD2 . PHE A 66  ? 0.0707 0.1769 0.1696 -0.0945 -0.0086 -0.0365 66  PHE A CD2 
564  C  CE1 . PHE A 66  ? 0.2293 0.1799 0.1878 -0.0523 -0.0603 -0.0756 66  PHE A CE1 
565  C  CE2 . PHE A 66  ? 0.2477 0.1706 0.1508 0.0227  0.0015  -0.0392 66  PHE A CE2 
566  C  CZ  . PHE A 66  ? 0.2718 0.1590 0.1508 -0.0274 -0.0212 -0.0518 66  PHE A CZ  
567  N  N   A GLN A 67  ? 0.0192 0.1877 0.1845 -0.0350 -0.0166 -0.0717 67  GLN A N   
568  N  N   B GLN A 67  ? 0.2294 0.1005 0.1388 -0.0086 -0.0873 -0.0610 67  GLN A N   
569  C  CA  A GLN A 67  ? 0.0290 0.1365 0.1815 -0.0384 -0.0229 -0.0609 67  GLN A CA  
570  C  CA  B GLN A 67  ? 0.1661 0.1369 0.1256 -0.0325 -0.0862 -0.0570 67  GLN A CA  
571  C  C   A GLN A 67  ? 0.0197 0.1257 0.1325 -0.0369 0.0058  -0.0619 67  GLN A C   
572  C  C   B GLN A 67  ? 0.1779 0.1338 0.1209 -0.0762 -0.0572 -0.0638 67  GLN A C   
573  O  O   A GLN A 67  ? 0.0318 0.1832 0.1443 -0.0663 0.0256  -0.0873 67  GLN A O   
574  O  O   B GLN A 67  ? 0.1381 0.1719 0.1304 -0.1287 -0.0068 -0.0622 67  GLN A O   
575  C  CB  A GLN A 67  ? 0.0554 0.1185 0.1620 -0.0218 0.0047  -0.0664 67  GLN A CB  
576  C  CB  B GLN A 67  ? 0.0441 0.1868 0.1373 -0.0179 -0.0491 -0.0842 67  GLN A CB  
577  C  CG  A GLN A 67  ? 0.0066 0.1605 0.2086 -0.0071 0.0046  -0.0667 67  GLN A CG  
578  C  CG  B GLN A 67  ? 0.0308 0.1546 0.1485 -0.0315 -0.0309 -0.0656 67  GLN A CG  
579  C  CD  A GLN A 67  ? 0.0183 0.2020 0.2320 -0.0144 -0.0428 -0.0621 67  GLN A CD  
580  C  CD  B GLN A 67  ? 0.0784 0.1493 0.2043 -0.0229 -0.0173 -0.0216 67  GLN A CD  
581  O  OE1 A GLN A 67  ? 0.0579 0.1905 0.2983 -0.0927 -0.0306 -0.0142 67  GLN A OE1 
582  O  OE1 B GLN A 67  ? 0.0635 0.1821 0.2470 -0.0143 0.0036  -0.0707 67  GLN A OE1 
583  N  NE2 A GLN A 67  ? 0.0118 0.2102 0.2728 -0.0300 0.0233  -0.0478 67  GLN A NE2 
584  N  NE2 B GLN A 67  ? 0.0972 0.1486 0.2096 -0.0414 -0.0145 -0.0234 67  GLN A NE2 
585  N  N   A VAL A 68  ? 0.0194 0.1584 0.1728 -0.0443 0.0149  -0.0642 68  VAL A N   
586  N  N   B VAL A 68  ? 0.1477 0.0843 0.1476 -0.0737 -0.0468 -0.0461 68  VAL A N   
587  C  CA  A VAL A 68  ? 0.0236 0.1585 0.1421 -0.0381 -0.0131 -0.0633 68  VAL A CA  
588  C  CA  B VAL A 68  ? 0.1585 0.1143 0.1540 -0.0641 -0.0713 -0.0660 68  VAL A CA  
589  C  C   A VAL A 68  ? 0.0084 0.1727 0.1803 -0.0074 -0.0134 -0.0636 68  VAL A C   
590  C  C   B VAL A 68  ? 0.0541 0.1195 0.1550 -0.0608 -0.0033 -0.0685 68  VAL A C   
591  O  O   A VAL A 68  ? 0.0931 0.1049 0.1870 -0.0684 -0.0491 -0.0438 68  VAL A O   
592  O  O   B VAL A 68  ? 0.1387 0.1159 0.1429 -0.0506 -0.0411 -0.0798 68  VAL A O   
593  C  CB  A VAL A 68  ? 0.0335 0.1109 0.2029 -0.0322 -0.0320 -0.0529 68  VAL A CB  
594  C  CB  B VAL A 68  ? 0.1549 0.1120 0.1811 -0.0720 -0.0736 -0.0630 68  VAL A CB  
595  C  CG1 A VAL A 68  ? 0.0142 0.1370 0.2191 -0.0287 0.0266  -0.0413 68  VAL A CG1 
596  C  CG1 B VAL A 68  ? 0.1477 0.0820 0.2560 -0.0108 -0.1292 -0.0893 68  VAL A CG1 
597  C  CG2 A VAL A 68  ? 0.0168 0.1136 0.1758 -0.0290 -0.0051 -0.0524 68  VAL A CG2 
598  C  CG2 B VAL A 68  ? 0.2405 0.1154 0.1675 -0.0540 -0.0906 -0.0721 68  VAL A CG2 
599  N  N   A GLU A 69  ? 0.0153 0.1340 0.1872 -0.0293 -0.0073 -0.0502 69  GLU A N   
600  N  N   B GLU A 69  ? 0.0403 0.1238 0.1291 -0.0212 -0.0254 -0.0882 69  GLU A N   
601  C  CA  A GLU A 69  ? 0.0173 0.1461 0.1238 -0.0209 -0.0190 -0.0550 69  GLU A CA  
602  C  CA  B GLU A 69  ? 0.0393 0.1500 0.1503 -0.0218 0.0004  -0.0472 69  GLU A CA  
603  C  C   A GLU A 69  ? 0.0536 0.1207 0.1100 -0.0660 0.0071  -0.0507 69  GLU A C   
604  C  C   B GLU A 69  ? 0.0575 0.1659 0.1539 -0.0182 -0.0330 -0.0952 69  GLU A C   
605  O  O   A GLU A 69  ? 0.0450 0.1139 0.1190 -0.0484 0.0163  -0.0582 69  GLU A O   
606  O  O   B GLU A 69  ? 0.0687 0.1386 0.1311 -0.0615 -0.0060 -0.0665 69  GLU A O   
607  C  CB  A GLU A 69  ? 0.0281 0.1580 0.1484 -0.0550 0.0328  -0.0487 69  GLU A CB  
608  C  CB  B GLU A 69  ? 0.0204 0.1805 0.1707 -0.0365 -0.0141 -0.0726 69  GLU A CB  
609  C  CG  A GLU A 69  ? 0.0141 0.1739 0.1321 -0.0337 0.0203  -0.0499 69  GLU A CG  
610  C  CG  B GLU A 69  ? 0.0123 0.1756 0.2113 -0.0317 0.0141  -0.0617 69  GLU A CG  
611  C  CD  A GLU A 69  ? 0.0247 0.1078 0.1637 -0.0320 0.0384  -0.0735 69  GLU A CD  
612  C  CD  B GLU A 69  ? 0.0511 0.1893 0.2125 -0.0095 0.0407  -0.0868 69  GLU A CD  
613  O  OE1 A GLU A 69  ? 0.0218 0.1482 0.1681 -0.0190 0.0162  -0.0753 69  GLU A OE1 
614  O  OE1 B GLU A 69  ? 0.0750 0.2248 0.1906 -0.0060 0.0369  -0.0897 69  GLU A OE1 
615  O  OE2 A GLU A 69  ? 0.0239 0.1526 0.2016 -0.0348 0.0561  -0.0746 69  GLU A OE2 
616  O  OE2 B GLU A 69  ? 0.0385 0.1604 0.2961 -0.0627 0.0024  -0.0868 69  GLU A OE2 
617  N  N   . PHE A 70  ? 0.2768 0.1356 0.1430 -0.0267 -0.0192 -0.0502 70  PHE A N   
618  C  CA  . PHE A 70  ? 0.3350 0.0870 0.2129 -0.0522 -0.0740 -0.0722 70  PHE A CA  
619  C  C   . PHE A 70  ? 0.3802 0.1018 0.2039 0.0020  -0.1062 -0.0697 70  PHE A C   
620  O  O   . PHE A 70  ? 0.2942 0.1005 0.2163 -0.0431 -0.0895 -0.0728 70  PHE A O   
621  C  CB  . PHE A 70  ? 0.2247 0.1155 0.2097 -0.0359 -0.1126 -0.0685 70  PHE A CB  
622  C  CG  . PHE A 70  ? 0.2557 0.1137 0.1998 -0.0288 -0.1226 -0.0736 70  PHE A CG  
623  C  CD1 . PHE A 70  ? 0.2630 0.1247 0.2151 -0.0361 -0.1095 -0.1078 70  PHE A CD1 
624  C  CD2 . PHE A 70  ? 0.2343 0.1238 0.2173 -0.0439 -0.1351 -0.0743 70  PHE A CD2 
625  C  CE1 . PHE A 70  ? 0.2490 0.1269 0.2318 -0.0462 -0.1093 -0.0774 70  PHE A CE1 
626  C  CE2 . PHE A 70  ? 0.2612 0.1107 0.2263 -0.0430 -0.1029 -0.1017 70  PHE A CE2 
627  C  CZ  . PHE A 70  ? 0.2412 0.1388 0.2087 -0.0579 -0.0580 -0.0795 70  PHE A CZ  
628  N  N   . ASP A 71  ? 0.4794 0.1137 0.2076 -0.0583 -0.1183 -0.0877 71  ASP A N   
629  C  CA  . ASP A 71  ? 0.3609 0.1125 0.2297 -0.0429 -0.0993 -0.1057 71  ASP A CA  
630  C  C   . ASP A 71  ? 0.3189 0.0983 0.2735 -0.0449 -0.0866 -0.0428 71  ASP A C   
631  O  O   . ASP A 71  ? 0.3966 0.2140 0.3063 0.0197  -0.0309 -0.0491 71  ASP A O   
632  C  CB  . ASP A 71  ? 0.3162 0.1138 0.2843 -0.0663 -0.0877 -0.0788 71  ASP A CB  
633  C  CG  . ASP A 71  ? 0.4439 0.1095 0.3695 -0.0787 -0.1767 -0.1054 71  ASP A CG  
634  O  OD1 . ASP A 71  ? 0.3231 0.1314 0.3008 -0.0599 -0.0495 -0.0937 71  ASP A OD1 
635  O  OD2 . ASP A 71  ? 0.4382 0.1924 0.4544 -0.0535 -0.2083 -0.0876 71  ASP A OD2 
636  N  N   . ASP A 72  ? 0.2472 0.1288 0.2512 -0.0354 -0.0410 -0.0515 72  ASP A N   
637  C  CA  . ASP A 72  ? 0.2320 0.1472 0.2859 -0.0732 -0.0510 -0.0179 72  ASP A CA  
638  C  C   . ASP A 72  ? 0.2496 0.1323 0.3097 -0.1063 -0.0913 -0.0326 72  ASP A C   
639  O  O   . ASP A 72  ? 0.3524 0.1219 0.2967 -0.0798 -0.0824 -0.0531 72  ASP A O   
640  C  CB  . ASP A 72  ? 0.2414 0.1166 0.2413 -0.0615 -0.0124 -0.0791 72  ASP A CB  
641  C  CG  . ASP A 72  ? 0.2379 0.1703 0.2658 -0.0561 -0.0549 -0.1031 72  ASP A CG  
642  O  OD1 . ASP A 72  ? 0.3630 0.1818 0.2516 -0.0469 -0.0814 -0.1021 72  ASP A OD1 
643  O  OD2 . ASP A 72  ? 0.2716 0.2052 0.2344 -0.0251 -0.0656 -0.0862 72  ASP A OD2 
644  N  N   . SER A 73  ? 0.1857 0.1188 0.3467 -0.0400 -0.1163 -0.0591 73  SER A N   
645  C  CA  . SER A 73  ? 0.3043 0.1147 0.3402 -0.0499 -0.0486 -0.0695 73  SER A CA  
646  C  C   . SER A 73  ? 0.2997 0.1430 0.3895 -0.0427 -0.0273 -0.0514 73  SER A C   
647  O  O   . SER A 73  ? 0.4394 0.1417 0.3170 -0.0272 -0.1039 -0.0633 73  SER A O   
648  C  CB  . SER A 73  ? 0.2475 0.2707 0.2861 -0.0771 -0.0561 -0.0496 73  SER A CB  
649  O  OG  . SER A 73  ? 0.2502 0.1543 0.3064 -0.0700 -0.0435 -0.0985 73  SER A OG  
650  N  N   . GLN A 74  ? 0.2389 0.1348 0.3673 -0.0792 -0.0783 -0.1063 74  GLN A N   
651  C  CA  . GLN A 74  ? 0.3177 0.1682 0.4433 -0.1239 -0.0684 -0.0480 74  GLN A CA  
652  C  C   . GLN A 74  ? 0.2813 0.2208 0.3165 -0.0961 -0.1215 -0.0431 74  GLN A C   
653  O  O   . GLN A 74  ? 0.1625 0.2131 0.3313 -0.0434 -0.0435 -0.0092 74  GLN A O   
654  C  CB  . GLN A 74  ? 0.3351 0.4705 0.4439 -0.2447 -0.0525 -0.0510 74  GLN A CB  
655  C  CG  . GLN A 74  ? 0.3638 0.5733 0.5250 0.0342  -0.0510 -0.1204 74  GLN A CG  
656  C  CD  . GLN A 74  ? 0.3249 0.5181 0.5264 -0.0886 -0.0300 -0.2045 74  GLN A CD  
657  O  OE1 . GLN A 74  ? 0.3452 0.9657 0.6512 0.0285  0.0708  -0.0683 74  GLN A OE1 
658  N  NE2 . GLN A 74  ? 0.1841 0.4593 0.5722 0.0574  0.0238  -0.0666 74  GLN A NE2 
659  N  N   . ASP A 75  ? 0.3305 0.2531 0.2963 -0.0738 -0.1223 -0.0757 75  ASP A N   
660  C  CA  . ASP A 75  ? 0.2356 0.2331 0.3682 -0.0714 -0.0620 -0.0520 75  ASP A CA  
661  C  C   . ASP A 75  ? 0.3386 0.2782 0.4759 -0.0925 -0.1497 0.0220  75  ASP A C   
662  O  O   . ASP A 75  ? 0.3128 0.6534 0.8155 -0.0381 -0.1436 0.0709  75  ASP A O   
663  C  CB  . ASP A 75  ? 0.2194 0.2602 0.4509 -0.1182 -0.0960 0.0187  75  ASP A CB  
664  C  CG  . ASP A 75  ? 0.0694 0.4015 0.5159 -0.0105 -0.0859 -0.0794 75  ASP A CG  
665  O  OD1 . ASP A 75  ? 0.1384 0.3778 0.4606 -0.1331 -0.0672 0.0310  75  ASP A OD1 
666  O  OD2 . ASP A 75  ? 0.4418 0.4757 0.5808 -0.1707 0.0232  -0.0674 75  ASP A OD2 
667  N  N   . LYS A 76  ? 0.1935 0.2205 0.3892 -0.0058 -0.1406 -0.0762 76  LYS A N   
668  C  CA  . LYS A 76  ? 0.1091 0.1764 0.4564 -0.0160 -0.0455 -0.0570 76  LYS A CA  
669  C  C   . LYS A 76  ? 0.2341 0.1975 0.6910 -0.0062 -0.0345 -0.1508 76  LYS A C   
670  O  O   . LYS A 76  ? 0.4552 0.4316 0.7433 -0.0866 -0.0053 -0.1487 76  LYS A O   
671  C  CB  . LYS A 76  ? 0.4062 0.2408 0.3611 -0.0385 -0.0861 -0.1231 76  LYS A CB  
672  C  CG  . LYS A 76  ? 0.2348 0.2933 0.3582 -0.0657 -0.0402 -0.1464 76  LYS A CG  
673  C  CD  . LYS A 76  ? 0.4051 0.3371 0.3714 -0.0779 0.0152  -0.1183 76  LYS A CD  
674  C  CE  . LYS A 76  ? 0.2592 0.2763 0.3591 -0.0867 0.0428  -0.0635 76  LYS A CE  
675  N  NZ  . LYS A 76  ? 0.4702 0.3159 0.3608 -0.2051 0.0702  -0.0653 76  LYS A NZ  
676  N  N   . ALA A 77  ? 0.2394 0.2890 0.4177 -0.0703 -0.0974 -0.1242 77  ALA A N   
677  C  CA  . ALA A 77  ? 0.1086 0.2289 0.3240 -0.0892 -0.1043 -0.0299 77  ALA A CA  
678  C  C   . ALA A 77  ? 0.0945 0.2136 0.2814 -0.0450 -0.1049 -0.0936 77  ALA A C   
679  O  O   . ALA A 77  ? 0.1192 0.2309 0.2543 -0.0214 -0.0514 -0.0401 77  ALA A O   
680  C  CB  . ALA A 77  ? 0.2059 0.3508 0.3445 -0.1619 -0.0490 -0.0105 77  ALA A CB  
681  N  N   . VAL A 78  ? 0.1428 0.1639 0.2637 -0.0395 -0.1008 -0.0419 78  VAL A N   
682  C  CA  . VAL A 78  ? 0.1278 0.1697 0.2556 -0.0048 -0.0685 -0.0597 78  VAL A CA  
683  C  C   . VAL A 78  ? 0.0484 0.1980 0.2483 -0.0271 -0.0613 -0.0661 78  VAL A C   
684  O  O   . VAL A 78  ? 0.0590 0.2142 0.3171 -0.0261 -0.0827 -0.0558 78  VAL A O   
685  C  CB  . VAL A 78  ? 0.0863 0.2279 0.3318 0.0042  -0.0477 -0.0289 78  VAL A CB  
686  C  CG1 . VAL A 78  ? 0.2309 0.1621 0.3586 -0.0241 -0.0403 -0.0311 78  VAL A CG1 
687  C  CG2 . VAL A 78  ? 0.1010 0.2516 0.3555 -0.0186 0.0006  -0.0223 78  VAL A CG2 
688  N  N   . LEU A 79  ? 0.0483 0.1521 0.2358 -0.0412 -0.0573 -0.0464 79  LEU A N   
689  C  CA  . LEU A 79  ? 0.0204 0.1663 0.2275 -0.0366 -0.0254 -0.0400 79  LEU A CA  
690  C  C   . LEU A 79  ? 0.0110 0.2023 0.2406 -0.0253 -0.0137 -0.0308 79  LEU A C   
691  O  O   . LEU A 79  ? 0.0498 0.1737 0.2531 -0.0305 0.0030  -0.0226 79  LEU A O   
692  C  CB  . LEU A 79  ? 0.0322 0.1452 0.3202 -0.0300 -0.0546 -0.0801 79  LEU A CB  
693  C  CG  . LEU A 79  ? 0.0357 0.1404 0.3160 -0.0478 -0.0294 -0.0776 79  LEU A CG  
694  C  CD1 . LEU A 79  ? 0.0397 0.1797 0.4224 -0.0089 0.0033  -0.0952 79  LEU A CD1 
695  C  CD2 . LEU A 79  ? 0.0238 0.1771 0.2054 -0.0525 -0.0015 -0.0411 79  LEU A CD2 
696  N  N   . LYS A 80  ? 0.0198 0.2081 0.2529 -0.0494 0.0103  -0.0350 80  LYS A N   
697  C  CA  . LYS A 80  ? 0.0867 0.1787 0.2705 -0.0137 0.0183  -0.0317 80  LYS A CA  
698  C  C   . LYS A 80  ? 0.0318 0.1874 0.2576 -0.0359 -0.0035 -0.0423 80  LYS A C   
699  O  O   . LYS A 80  ? 0.0101 0.1839 0.3222 -0.0259 0.0060  -0.0449 80  LYS A O   
700  C  CB  . LYS A 80  ? 0.2188 0.2253 0.3664 -0.0996 0.0200  -0.0603 80  LYS A CB  
701  C  CG  . LYS A 80  ? 0.4530 0.2451 0.6764 -0.2388 -0.2284 -0.1257 80  LYS A CG  
702  C  CD  . LYS A 80  ? 0.6254 2.0394 1.9649 -1.0084 -0.3580 -0.2433 80  LYS A CD  
703  C  CE  . LYS A 80  ? 0.2060 0.9951 0.8805 -0.1093 -0.4140 0.2312  80  LYS A CE  
704  N  NZ  . LYS A 80  ? 0.4026 0.4050 0.6648 0.0348  -0.0282 0.0490  80  LYS A NZ  
705  N  N   . GLY A 81  ? 0.0432 0.2128 0.2825 -0.0487 0.0436  -0.0441 81  GLY A N   
706  C  CA  . GLY A 81  ? 0.0604 0.1918 0.3553 -0.0751 0.0717  -0.0861 81  GLY A CA  
707  C  C   . GLY A 81  ? 0.0541 0.2039 0.4268 -0.0842 0.0851  -0.0354 81  GLY A C   
708  O  O   . GLY A 81  ? 0.0221 0.1947 0.2749 -0.0271 0.0388  0.0024  81  GLY A O   
709  N  N   . GLY A 82  ? 0.0266 0.2447 0.5786 -0.0682 0.0433  -0.0765 82  GLY A N   
710  C  CA  . GLY A 82  ? 0.0520 0.1793 0.5800 -0.0661 0.0619  -0.1632 82  GLY A CA  
711  C  C   . GLY A 82  ? 0.0773 0.2309 0.3730 -0.1224 0.0864  -0.1552 82  GLY A C   
712  O  O   . GLY A 82  ? 0.2500 0.4854 0.3701 -0.2125 0.1321  -0.1646 82  GLY A O   
713  N  N   . PRO A 83  ? 0.0603 0.1974 0.3318 -0.0724 0.0854  -0.0678 83  PRO A N   
714  C  CA  . PRO A 83  ? 0.1321 0.1960 0.2339 -0.0833 0.0893  -0.0540 83  PRO A CA  
715  C  C   . PRO A 83  ? 0.1161 0.1938 0.2260 -0.0990 0.0632  -0.0182 83  PRO A C   
716  O  O   . PRO A 83  ? 0.1738 0.2811 0.2790 -0.1051 -0.0036 -0.0334 83  PRO A O   
717  C  CB  . PRO A 83  ? 0.1073 0.1955 0.2248 -0.0750 0.0695  -0.0609 83  PRO A CB  
718  C  CG  . PRO A 83  ? 0.0281 0.1925 0.2738 -0.0509 0.0555  -0.0386 83  PRO A CG  
719  C  CD  . PRO A 83  ? 0.0339 0.2182 0.3276 -0.0504 0.0765  -0.0262 83  PRO A CD  
720  N  N   . LEU A 84  ? 0.0314 0.1786 0.2244 -0.0622 0.0301  -0.0178 84  LEU A N   
721  C  CA  . LEU A 84  ? 0.0615 0.1585 0.2548 -0.0669 0.0514  0.0030  84  LEU A CA  
722  C  C   . LEU A 84  ? 0.0502 0.2324 0.3447 -0.0917 0.0421  0.0127  84  LEU A C   
723  O  O   . LEU A 84  ? 0.1052 0.3292 0.4609 -0.1676 0.0506  0.0419  84  LEU A O   
724  C  CB  . LEU A 84  ? 0.0441 0.1516 0.2633 -0.0715 0.0306  -0.0093 84  LEU A CB  
725  C  CG  . LEU A 84  ? 0.0451 0.1452 0.2582 -0.0712 0.0336  -0.0199 84  LEU A CG  
726  C  CD1 . LEU A 84  ? 0.0513 0.2230 0.2551 -0.0955 0.0277  -0.0031 84  LEU A CD1 
727  C  CD2 . LEU A 84  ? 0.0296 0.1621 0.2649 -0.0458 0.0556  -0.0191 84  LEU A CD2 
728  N  N   . ASP A 85  ? 0.0730 0.1901 0.2707 -0.0979 0.0259  0.0058  85  ASP A N   
729  C  CA  . ASP A 85  ? 0.1310 0.1883 0.3180 -0.0520 0.0370  0.0241  85  ASP A CA  
730  C  C   . ASP A 85  ? 0.1888 0.1430 0.4088 -0.0769 0.1105  -0.0402 85  ASP A C   
731  O  O   . ASP A 85  ? 0.1966 0.3186 0.4881 -0.0785 0.1395  -0.0002 85  ASP A O   
732  C  CB  . ASP A 85  ? 0.2699 0.2739 0.3648 -0.0850 -0.0248 0.0839  85  ASP A CB  
733  C  CG  . ASP A 85  ? 0.3635 0.3975 0.4153 -0.1162 -0.0066 0.0672  85  ASP A CG  
734  O  OD1 . ASP A 85  ? 0.4713 0.5289 0.5479 0.0055  -0.0889 0.0350  85  ASP A OD1 
735  O  OD2 . ASP A 85  ? 0.3491 0.5296 0.5026 -0.1239 -0.0776 0.0307  85  ASP A OD2 
736  N  N   . GLY A 86  ? 0.1860 0.3003 0.4412 -0.1109 0.0554  0.0254  86  GLY A N   
737  C  CA  . GLY A 86  ? 0.2468 0.2504 0.4109 -0.0222 0.0129  0.0348  86  GLY A CA  
738  C  C   . GLY A 86  ? 0.1596 0.2053 0.2869 -0.0369 -0.0428 -0.0519 86  GLY A C   
739  O  O   . GLY A 86  ? 0.3659 0.2679 0.2847 0.0942  -0.0010 -0.0079 86  GLY A O   
740  N  N   . THR A 87  ? 0.0703 0.1758 0.3054 -0.0881 0.0043  -0.0588 87  THR A N   
741  C  CA  . THR A 87  ? 0.0352 0.1931 0.3334 -0.0724 -0.0108 -0.0124 87  THR A CA  
742  C  C   . THR A 87  ? 0.0289 0.1592 0.3193 -0.0573 -0.0182 0.0006  87  THR A C   
743  O  O   . THR A 87  ? 0.0655 0.0902 0.2887 -0.0658 -0.0220 -0.0227 87  THR A O   
744  C  CB  . THR A 87  ? 0.2381 0.4104 0.4542 -0.1587 -0.0335 -0.1237 87  THR A CB  
745  O  OG1 . THR A 87  ? 0.2093 0.7099 0.7465 -0.2074 -0.0019 0.0948  87  THR A OG1 
746  C  CG2 . THR A 87  ? 0.2885 0.4524 0.4968 -0.1659 -0.0002 0.0463  87  THR A CG2 
747  N  N   . TYR A 88  ? 0.0360 0.1397 0.2701 -0.0605 -0.0141 -0.0208 88  TYR A N   
748  C  CA  . TYR A 88  ? 0.0399 0.1464 0.2638 -0.0625 -0.0280 -0.0217 88  TYR A CA  
749  C  C   . TYR A 88  ? 0.0351 0.1405 0.2590 -0.0457 -0.0256 -0.0259 88  TYR A C   
750  O  O   . TYR A 88  ? 0.0788 0.1461 0.3309 -0.0262 -0.0914 -0.0952 88  TYR A O   
751  C  CB  . TYR A 88  ? 0.0694 0.0973 0.2128 -0.0366 -0.0356 -0.0245 88  TYR A CB  
752  C  CG  . TYR A 88  ? 0.0532 0.1150 0.2061 -0.0683 -0.0127 -0.0236 88  TYR A CG  
753  C  CD1 . TYR A 88  ? 0.0522 0.1215 0.1778 -0.0392 0.0030  -0.0135 88  TYR A CD1 
754  C  CD2 . TYR A 88  ? 0.0518 0.1088 0.1809 -0.0639 -0.0010 -0.0453 88  TYR A CD2 
755  C  CE1 . TYR A 88  ? 0.0424 0.1446 0.1780 -0.0698 0.0254  -0.0279 88  TYR A CE1 
756  C  CE2 . TYR A 88  ? 0.0362 0.0990 0.1806 -0.0487 -0.0022 -0.0437 88  TYR A CE2 
757  C  CZ  . TYR A 88  ? 0.0200 0.1000 0.1674 -0.0358 0.0082  -0.0296 88  TYR A CZ  
758  O  OH  . TYR A 88  ? 0.0181 0.1357 0.1815 -0.0381 0.0134  -0.0120 88  TYR A OH  
759  N  N   . ARG A 89  ? 0.0588 0.1114 0.2270 -0.0661 -0.0307 -0.0122 89  ARG A N   
760  C  CA  . ARG A 89  ? 0.1104 0.0824 0.2437 -0.0465 -0.0611 -0.0411 89  ARG A CA  
761  C  C   . ARG A 89  ? 0.0802 0.0895 0.2141 -0.0487 -0.0420 -0.0691 89  ARG A C   
762  O  O   . ARG A 89  ? 0.0773 0.0994 0.1858 -0.0487 -0.0452 -0.0638 89  ARG A O   
763  C  CB  . ARG A 89  ? 0.2000 0.0976 0.2890 -0.0412 -0.1057 -0.0928 89  ARG A CB  
764  C  CG  . ARG A 89  ? 0.2312 0.1438 0.3407 -0.0873 0.0149  -0.1024 89  ARG A CG  
765  C  CD  . ARG A 89  ? 0.3419 0.1696 0.3425 -0.1040 -0.0511 -0.1705 89  ARG A CD  
766  N  NE  . ARG A 89  ? 0.3067 0.2295 0.2909 -0.0741 -0.1221 -0.0447 89  ARG A NE  
767  C  CZ  . ARG A 89  ? 0.1877 0.2330 0.3200 -0.0602 -0.0526 -0.0666 89  ARG A CZ  
768  N  NH1 . ARG A 89  ? 0.2236 0.2030 0.3308 -0.1072 -0.0644 -0.0307 89  ARG A NH1 
769  N  NH2 . ARG A 89  ? 0.3259 0.4619 0.4721 -0.2322 -0.0641 0.0527  89  ARG A NH2 
770  N  N   . LEU A 90  ? 0.0669 0.1049 0.1945 -0.0385 -0.0533 -0.0653 90  LEU A N   
771  C  CA  . LEU A 90  ? 0.0951 0.1121 0.2083 -0.0342 -0.0557 -0.0510 90  LEU A CA  
772  C  C   . LEU A 90  ? 0.0737 0.1021 0.1974 -0.0280 -0.0634 -0.0579 90  LEU A C   
773  O  O   . LEU A 90  ? 0.1606 0.1445 0.2072 -0.0510 -0.0741 -0.0805 90  LEU A O   
774  C  CB  . LEU A 90  ? 0.1218 0.1044 0.2537 -0.0167 -0.0854 -0.0635 90  LEU A CB  
775  C  CG  . LEU A 90  ? 0.1850 0.1207 0.1963 -0.0257 -0.0709 -0.0624 90  LEU A CG  
776  C  CD1 . LEU A 90  ? 0.2469 0.0990 0.2074 -0.0498 -0.0716 -0.0557 90  LEU A CD1 
777  C  CD2 . LEU A 90  ? 0.1703 0.1643 0.2761 -0.0242 -0.0789 -0.0354 90  LEU A CD2 
778  N  N   . LEU A 91  ? 0.0897 0.1142 0.1690 -0.0401 -0.0427 -0.0395 91  LEU A N   
779  C  CA  . LEU A 91  ? 0.0969 0.1333 0.1655 -0.0526 -0.0290 -0.0336 91  LEU A CA  
780  C  C   . LEU A 91  ? 0.1397 0.0850 0.1546 -0.0222 -0.0433 -0.0600 91  LEU A C   
781  O  O   . LEU A 91  ? 0.1570 0.1148 0.1437 -0.0043 -0.0581 -0.0525 91  LEU A O   
782  C  CB  . LEU A 91  ? 0.1459 0.1532 0.1986 -0.0430 -0.0605 -0.0177 91  LEU A CB  
783  C  CG  . LEU A 91  ? 0.1280 0.1220 0.2230 -0.0441 -0.0547 -0.0339 91  LEU A CG  
784  C  CD1 . LEU A 91  ? 0.1815 0.1728 0.4271 0.0109  -0.0876 -0.1590 91  LEU A CD1 
785  C  CD2 . LEU A 91  ? 0.0642 0.3078 0.3215 -0.0499 -0.0361 0.0297  91  LEU A CD2 
786  N  N   A GLN A 92  ? 0.1751 0.0890 0.1547 -0.0236 -0.0284 -0.0707 92  GLN A N   
787  N  N   B GLN A 92  ? 0.1725 0.0881 0.1515 -0.0194 -0.0330 -0.0692 92  GLN A N   
788  C  CA  A GLN A 92  ? 0.2169 0.0863 0.1756 -0.0375 -0.0275 -0.0694 92  GLN A CA  
789  C  CA  B GLN A 92  ? 0.1989 0.0872 0.1610 -0.0368 -0.0366 -0.0734 92  GLN A CA  
790  C  C   A GLN A 92  ? 0.1470 0.0939 0.1307 -0.0348 -0.0132 -0.0580 92  GLN A C   
791  C  C   B GLN A 92  ? 0.1649 0.0859 0.1357 -0.0406 -0.0258 -0.0587 92  GLN A C   
792  O  O   A GLN A 92  ? 0.0818 0.0929 0.1319 -0.0336 -0.0436 -0.0599 92  GLN A O   
793  O  O   B GLN A 92  ? 0.0798 0.0861 0.1307 -0.0384 -0.0318 -0.0646 92  GLN A O   
794  C  CB  A GLN A 92  ? 0.2182 0.1291 0.1454 -0.0185 -0.0259 -0.0529 92  GLN A CB  
795  C  CB  B GLN A 92  ? 0.1870 0.0894 0.1456 -0.0044 -0.0380 -0.0889 92  GLN A CB  
796  C  CG  A GLN A 92  ? 0.1758 0.0836 0.1942 -0.0577 -0.0366 -0.0531 92  GLN A CG  
797  C  CG  B GLN A 92  ? 0.1376 0.1394 0.1354 0.0223  -0.0209 -0.0621 92  GLN A CG  
798  C  CD  A GLN A 92  ? 0.0274 0.0967 0.1918 -0.0242 -0.0238 -0.0653 92  GLN A CD  
799  C  CD  B GLN A 92  ? 0.1236 0.1281 0.1749 -0.0317 -0.0576 -0.0983 92  GLN A CD  
800  O  OE1 A GLN A 92  ? 0.1016 0.0824 0.1416 -0.0324 -0.0452 -0.0653 92  GLN A OE1 
801  O  OE1 B GLN A 92  ? 0.2010 0.1274 0.1819 0.0179  -0.0287 -0.0778 92  GLN A OE1 
802  N  NE2 A GLN A 92  ? 0.0517 0.1483 0.2565 0.0004  0.0277  -0.0346 92  GLN A NE2 
803  N  NE2 B GLN A 92  ? 0.1927 0.1417 0.1438 -0.0416 -0.0411 -0.1180 92  GLN A NE2 
804  N  N   . PHE A 93  ? 0.2051 0.0928 0.1150 -0.0438 -0.0362 -0.0587 93  PHE A N   
805  C  CA  . PHE A 93  ? 0.1543 0.0881 0.1386 -0.0277 -0.0511 -0.0639 93  PHE A CA  
806  C  C   . PHE A 93  ? 0.1652 0.0772 0.1230 -0.0018 -0.0474 -0.0605 93  PHE A C   
807  O  O   . PHE A 93  ? 0.2197 0.1098 0.1273 -0.0209 -0.0373 -0.0546 93  PHE A O   
808  C  CB  . PHE A 93  ? 0.1301 0.1046 0.1939 -0.0195 -0.0888 -0.0663 93  PHE A CB  
809  C  CG  . PHE A 93  ? 0.1486 0.1028 0.1908 -0.0126 -0.0703 -0.0709 93  PHE A CG  
810  C  CD1 . PHE A 93  ? 0.1952 0.1087 0.1822 -0.0475 -0.0802 -0.0681 93  PHE A CD1 
811  C  CD2 . PHE A 93  ? 0.2129 0.1335 0.1988 -0.0377 -0.1286 -0.0866 93  PHE A CD2 
812  C  CE1 . PHE A 93  ? 0.1420 0.1360 0.1915 -0.0118 -0.0828 -0.0612 93  PHE A CE1 
813  C  CE2 . PHE A 93  ? 0.2408 0.1213 0.2146 -0.0447 -0.1294 -0.0549 93  PHE A CE2 
814  C  CZ  . PHE A 93  ? 0.2230 0.1280 0.2127 -0.0424 -0.1429 -0.0574 93  PHE A CZ  
815  N  N   . HIS A 94  ? 0.1592 0.0687 0.1436 -0.0232 -0.0376 -0.0509 94  HIS A N   
816  C  CA  . HIS A 94  ? 0.1220 0.0732 0.1246 -0.0157 -0.0477 -0.0562 94  HIS A CA  
817  C  C   . HIS A 94  ? 0.0717 0.0766 0.0947 -0.0269 -0.0260 -0.0475 94  HIS A C   
818  O  O   . HIS A 94  ? 0.0816 0.0848 0.1179 -0.0350 -0.0075 -0.0529 94  HIS A O   
819  C  CB  . HIS A 94  ? 0.1228 0.0825 0.1237 -0.0238 -0.0291 -0.0683 94  HIS A CB  
820  C  CG  . HIS A 94  ? 0.1021 0.1010 0.1059 -0.0080 -0.0181 -0.0585 94  HIS A CG  
821  N  ND1 . HIS A 94  ? 0.0904 0.0996 0.1123 -0.0193 -0.0103 -0.0577 94  HIS A ND1 
822  C  CD2 . HIS A 94  ? 0.0550 0.0890 0.1125 -0.0308 -0.0015 -0.0469 94  HIS A CD2 
823  C  CE1 . HIS A 94  ? 0.0861 0.0759 0.1051 -0.0122 -0.0059 -0.0450 94  HIS A CE1 
824  N  NE2 . HIS A 94  ? 0.0322 0.0825 0.0951 -0.0201 -0.0077 -0.0518 94  HIS A NE2 
825  N  N   . PHE A 95  ? 0.0662 0.0825 0.1292 -0.0340 -0.0253 -0.0549 95  PHE A N   
826  C  CA  . PHE A 95  ? 0.0304 0.0933 0.1229 -0.0244 -0.0164 -0.0642 95  PHE A CA  
827  C  C   . PHE A 95  ? 0.0221 0.0863 0.1035 -0.0241 -0.0044 -0.0474 95  PHE A C   
828  O  O   . PHE A 95  ? 0.0520 0.0978 0.1278 -0.0174 0.0115  -0.0580 95  PHE A O   
829  C  CB  . PHE A 95  ? 0.0386 0.1186 0.1342 -0.0275 -0.0111 -0.0508 95  PHE A CB  
830  C  CG  . PHE A 95  ? 0.0401 0.0994 0.1266 -0.0265 -0.0200 -0.0380 95  PHE A CG  
831  C  CD1 . PHE A 95  ? 0.0554 0.1229 0.1322 -0.0182 -0.0222 -0.0519 95  PHE A CD1 
832  C  CD2 . PHE A 95  ? 0.0642 0.0952 0.1326 -0.0183 -0.0097 -0.0301 95  PHE A CD2 
833  C  CE1 . PHE A 95  ? 0.0570 0.1451 0.1668 -0.0385 -0.0308 -0.0209 95  PHE A CE1 
834  C  CE2 . PHE A 95  ? 0.0778 0.1098 0.1721 -0.0388 -0.0273 -0.0231 95  PHE A CE2 
835  C  CZ  . PHE A 95  ? 0.0296 0.1529 0.1852 -0.0458 -0.0321 -0.0233 95  PHE A CZ  
836  N  N   . HIS A 96  ? 0.0615 0.0793 0.1167 -0.0312 -0.0100 -0.0469 96  HIS A N   
837  C  CA  . HIS A 96  ? 0.0220 0.0989 0.1156 -0.0194 0.0053  -0.0419 96  HIS A CA  
838  C  C   . HIS A 96  ? 0.0114 0.0988 0.1137 -0.0179 -0.0033 -0.0427 96  HIS A C   
839  O  O   . HIS A 96  ? 0.0136 0.0894 0.1354 -0.0238 0.0080  -0.0505 96  HIS A O   
840  C  CB  . HIS A 96  ? 0.0594 0.0790 0.1061 -0.0189 0.0116  -0.0530 96  HIS A CB  
841  C  CG  . HIS A 96  ? 0.0217 0.0915 0.1075 -0.0344 0.0057  -0.0405 96  HIS A CG  
842  N  ND1 . HIS A 96  ? 0.0235 0.0818 0.1190 -0.0353 0.0149  -0.0464 96  HIS A ND1 
843  C  CD2 . HIS A 96  ? 0.0304 0.0884 0.1118 -0.0395 0.0132  -0.0418 96  HIS A CD2 
844  C  CE1 . HIS A 96  ? 0.0205 0.0858 0.1175 -0.0335 0.0233  -0.0572 96  HIS A CE1 
845  N  NE2 . HIS A 96  ? 0.0322 0.0667 0.1085 -0.0395 0.0285  -0.0444 96  HIS A NE2 
846  N  N   . TRP A 97  ? 0.0546 0.0759 0.1005 -0.0157 0.0172  -0.0447 97  TRP A N   
847  C  CA  . TRP A 97  ? 0.0256 0.0759 0.1445 -0.0252 0.0111  -0.0428 97  TRP A CA  
848  C  C   . TRP A 97  ? 0.0220 0.0858 0.1064 -0.0221 0.0258  -0.0384 97  TRP A C   
849  O  O   . TRP A 97  ? 0.0205 0.1019 0.1279 -0.0247 0.0303  -0.0363 97  TRP A O   
850  C  CB  . TRP A 97  ? 0.0393 0.0973 0.1265 -0.0087 0.0242  -0.0279 97  TRP A CB  
851  C  CG  . TRP A 97  ? 0.0493 0.1032 0.1143 -0.0395 0.0071  -0.0502 97  TRP A CG  
852  C  CD1 . TRP A 97  ? 0.0626 0.1390 0.1308 -0.0145 0.0464  -0.0328 97  TRP A CD1 
853  C  CD2 . TRP A 97  ? 0.0700 0.0929 0.1177 -0.0172 0.0044  -0.0414 97  TRP A CD2 
854  N  NE1 . TRP A 97  ? 0.1407 0.1059 0.1217 -0.0019 0.0227  -0.0417 97  TRP A NE1 
855  C  CE2 . TRP A 97  ? 0.0919 0.1098 0.1165 -0.0037 0.0142  -0.0391 97  TRP A CE2 
856  C  CE3 . TRP A 97  ? 0.0901 0.0956 0.1198 -0.0172 -0.0021 -0.0445 97  TRP A CE3 
857  C  CZ2 . TRP A 97  ? 0.1315 0.1221 0.1113 -0.0120 0.0093  -0.0505 97  TRP A CZ2 
858  C  CZ3 . TRP A 97  ? 0.1143 0.1122 0.1213 -0.0108 0.0058  -0.0532 97  TRP A CZ3 
859  C  CH2 . TRP A 97  ? 0.1601 0.0960 0.1274 0.0116  0.0162  -0.0548 97  TRP A CH2 
860  N  N   . GLY A 98  ? 0.0549 0.0888 0.1311 -0.0282 0.0229  -0.0322 98  GLY A N   
861  C  CA  . GLY A 98  ? 0.0209 0.0976 0.1640 -0.0171 0.0410  -0.0381 98  GLY A CA  
862  C  C   . GLY A 98  ? 0.0646 0.0942 0.1408 -0.0223 0.0306  -0.0494 98  GLY A C   
863  O  O   . GLY A 98  ? 0.0778 0.0922 0.1416 -0.0216 0.0196  -0.0312 98  GLY A O   
864  N  N   . SER A 99  ? 0.0466 0.1186 0.1439 -0.0244 0.0319  -0.0286 99  SER A N   
865  C  CA  . SER A 99  ? 0.0624 0.1331 0.1457 -0.0212 0.0394  -0.0260 99  SER A CA  
866  C  C   . SER A 99  ? 0.0378 0.1125 0.1764 -0.0443 0.0209  -0.0102 99  SER A C   
867  O  O   . SER A 99  ? 0.0951 0.1721 0.1760 -0.0295 0.0099  -0.0024 99  SER A O   
868  C  CB  . SER A 99  ? 0.0508 0.1546 0.1716 -0.0086 0.0484  -0.0082 99  SER A CB  
869  O  OG  . SER A 99  ? 0.0480 0.1385 0.1967 -0.0354 0.0337  -0.0179 99  SER A OG  
870  N  N   . LEU A 100 ? 0.0353 0.1024 0.1699 -0.0384 0.0171  -0.0376 100 LEU A N   
871  C  CA  . LEU A 100 ? 0.0480 0.1094 0.2225 -0.0395 0.0453  -0.0328 100 LEU A CA  
872  C  C   . LEU A 100 ? 0.0286 0.1001 0.1837 -0.0446 0.0107  -0.0480 100 LEU A C   
873  O  O   . LEU A 100 ? 0.0863 0.1136 0.1846 -0.0250 0.0253  -0.0284 100 LEU A O   
874  C  CB  . LEU A 100 ? 0.0852 0.1587 0.3529 -0.0900 0.0991  -0.1123 100 LEU A CB  
875  C  CG  . LEU A 100 ? 0.0683 0.2180 0.3667 -0.0935 0.0524  -0.0825 100 LEU A CG  
876  C  CD1 . LEU A 100 ? 0.1730 0.3396 0.3285 -0.1480 0.0579  -0.1008 100 LEU A CD1 
877  C  CD2 . LEU A 100 ? 0.1429 0.2061 0.3982 -0.0278 0.1289  0.0094  100 LEU A CD2 
878  N  N   . ASP A 101 ? 0.0283 0.1086 0.1606 -0.0284 0.0025  -0.0469 101 ASP A N   
879  C  CA  . ASP A 101 ? 0.0561 0.0892 0.1849 -0.0455 0.0176  -0.0471 101 ASP A CA  
880  C  C   . ASP A 101 ? 0.0481 0.0832 0.1830 -0.0324 0.0115  -0.0530 101 ASP A C   
881  O  O   . ASP A 101 ? 0.1136 0.1034 0.2067 -0.0632 0.0279  -0.0519 101 ASP A O   
882  C  CB  . ASP A 101 ? 0.0608 0.1254 0.2049 -0.0149 -0.0002 -0.0614 101 ASP A CB  
883  C  CG  . ASP A 101 ? 0.0603 0.1908 0.2145 -0.0013 -0.0019 -0.0683 101 ASP A CG  
884  O  OD1 . ASP A 101 ? 0.0902 0.1368 0.2165 -0.0336 -0.0089 -0.0512 101 ASP A OD1 
885  O  OD2 . ASP A 101 ? 0.1764 0.2486 0.2548 0.0745  -0.0684 -0.1108 101 ASP A OD2 
886  N  N   . GLY A 102 ? 0.0649 0.0868 0.1870 -0.0335 -0.0066 -0.0570 102 GLY A N   
887  C  CA  . GLY A 102 ? 0.0757 0.1282 0.1902 -0.0036 0.0093  -0.0569 102 GLY A CA  
888  C  C   . GLY A 102 ? 0.0256 0.1116 0.1730 -0.0295 0.0102  -0.0495 102 GLY A C   
889  O  O   . GLY A 102 ? 0.0662 0.1179 0.1780 -0.0334 0.0117  -0.0558 102 GLY A O   
890  N  N   A GLN A 103 ? 0.0332 0.1017 0.1665 -0.0380 0.0432  -0.0397 103 GLN A N   
891  N  N   B GLN A 103 ? 0.0401 0.1129 0.1979 -0.0462 0.0471  -0.0579 103 GLN A N   
892  C  CA  A GLN A 103 ? 0.0107 0.1098 0.1272 -0.0213 0.0135  -0.0645 103 GLN A CA  
893  C  CA  B GLN A 103 ? 0.0500 0.1098 0.1816 -0.0472 0.0208  -0.0637 103 GLN A CA  
894  C  C   A GLN A 103 ? 0.0133 0.0930 0.1143 -0.0214 0.0241  -0.0521 103 GLN A C   
895  C  C   B GLN A 103 ? 0.0220 0.0930 0.1538 -0.0304 0.0428  -0.0543 103 GLN A C   
896  O  O   A GLN A 103 ? 0.0233 0.0813 0.1046 -0.0049 0.0264  -0.0518 103 GLN A O   
897  O  O   B GLN A 103 ? 0.0415 0.1165 0.1268 -0.0423 0.0610  -0.0444 103 GLN A O   
898  C  CB  A GLN A 103 ? 0.0309 0.1203 0.1318 -0.0471 0.0491  -0.0694 103 GLN A CB  
899  C  CB  B GLN A 103 ? 0.0504 0.1542 0.1339 -0.0521 0.0509  -0.0449 103 GLN A CB  
900  C  CG  A GLN A 103 ? 0.0608 0.1166 0.1523 -0.0739 0.0517  -0.0389 103 GLN A CG  
901  C  CG  B GLN A 103 ? 0.0639 0.1222 0.1603 -0.0606 0.0653  -0.0357 103 GLN A CG  
902  C  CD  A GLN A 103 ? 0.0528 0.1152 0.1893 -0.0654 0.0768  -0.0777 103 GLN A CD  
903  C  CD  B GLN A 103 ? 0.0687 0.1831 0.2790 -0.0773 0.0872  -0.0206 103 GLN A CD  
904  O  OE1 A GLN A 103 ? 0.0651 0.0860 0.2660 -0.0635 0.1023  -0.0811 103 GLN A OE1 
905  O  OE1 B GLN A 103 ? 0.0566 0.3598 0.3471 -0.1104 0.0866  -0.0444 103 GLN A OE1 
906  N  NE2 A GLN A 103 ? 0.0785 0.0849 0.2136 -0.0609 0.1026  -0.0665 103 GLN A NE2 
907  N  NE2 B GLN A 103 ? 0.0347 0.2159 0.4778 -0.0769 0.0400  -0.1267 103 GLN A NE2 
908  N  N   . GLY A 104 ? 0.0176 0.0943 0.1369 -0.0310 0.0211  -0.0442 104 GLY A N   
909  C  CA  . GLY A 104 ? 0.0125 0.0954 0.1183 -0.0226 0.0040  -0.0401 104 GLY A CA  
910  C  C   . GLY A 104 ? 0.0117 0.1039 0.1243 -0.0224 0.0156  -0.0479 104 GLY A C   
911  O  O   . GLY A 104 ? 0.0135 0.1040 0.1453 -0.0264 0.0147  -0.0479 104 GLY A O   
912  N  N   . SER A 105 ? 0.0135 0.0927 0.1070 -0.0247 0.0141  -0.0411 105 SER A N   
913  C  CA  . SER A 105 ? 0.0102 0.1067 0.1071 -0.0196 0.0077  -0.0328 105 SER A CA  
914  C  C   . SER A 105 ? 0.0195 0.0883 0.1093 -0.0307 0.0044  -0.0421 105 SER A C   
915  O  O   . SER A 105 ? 0.0194 0.0978 0.1391 -0.0323 0.0019  -0.0439 105 SER A O   
916  C  CB  . SER A 105 ? 0.0176 0.0860 0.1158 -0.0299 0.0189  -0.0488 105 SER A CB  
917  O  OG  . SER A 105 ? 0.0179 0.0850 0.1369 -0.0297 0.0163  -0.0566 105 SER A OG  
918  N  N   . GLU A 106 ? 0.0137 0.0809 0.1024 -0.0233 0.0149  -0.0396 106 GLU A N   
919  C  CA  . GLU A 106 ? 0.0261 0.0884 0.1213 -0.0379 0.0002  -0.0328 106 GLU A CA  
920  C  C   . GLU A 106 ? 0.0225 0.0894 0.1174 -0.0351 0.0030  -0.0334 106 GLU A C   
921  O  O   . GLU A 106 ? 0.0175 0.1005 0.1231 -0.0323 0.0133  -0.0449 106 GLU A O   
922  C  CB  . GLU A 106 ? 0.0174 0.0944 0.1104 -0.0309 0.0212  -0.0512 106 GLU A CB  
923  C  CG  . GLU A 106 ? 0.0315 0.0960 0.1177 -0.0379 0.0164  -0.0527 106 GLU A CG  
924  C  CD  . GLU A 106 ? 0.0233 0.1002 0.1155 -0.0377 0.0317  -0.0487 106 GLU A CD  
925  O  OE1 . GLU A 106 ? 0.0176 0.1014 0.1327 -0.0326 0.0135  -0.0328 106 GLU A OE1 
926  O  OE2 . GLU A 106 ? 0.0202 0.1312 0.1402 -0.0377 0.0288  -0.0379 106 GLU A OE2 
927  N  N   . HIS A 107 ? 0.0207 0.0800 0.1227 -0.0309 0.0093  -0.0477 107 HIS A N   
928  C  CA  . HIS A 107 ? 0.0202 0.0977 0.1239 -0.0355 0.0193  -0.0491 107 HIS A CA  
929  C  C   . HIS A 107 ? 0.0222 0.1051 0.1228 -0.0395 0.0248  -0.0584 107 HIS A C   
930  O  O   . HIS A 107 ? 0.0246 0.0914 0.1317 -0.0388 0.0197  -0.0574 107 HIS A O   
931  C  CB  . HIS A 107 ? 0.0207 0.1176 0.1260 -0.0396 0.0100  -0.0423 107 HIS A CB  
932  C  CG  . HIS A 107 ? 0.0273 0.1256 0.1382 -0.0501 0.0278  -0.0683 107 HIS A CG  
933  N  ND1 . HIS A 107 ? 0.0308 0.1116 0.1097 -0.0506 0.0188  -0.0467 107 HIS A ND1 
934  C  CD2 . HIS A 107 ? 0.0364 0.1391 0.1705 -0.0611 0.0395  -0.0502 107 HIS A CD2 
935  C  CE1 . HIS A 107 ? 0.0371 0.1212 0.1263 -0.0562 -0.0006 -0.0376 107 HIS A CE1 
936  N  NE2 . HIS A 107 ? 0.0235 0.1175 0.1138 -0.0431 0.0110  -0.0107 107 HIS A NE2 
937  N  N   . THR A 108 ? 0.0181 0.0970 0.1152 -0.0326 0.0148  -0.0456 108 THR A N   
938  C  CA  . THR A 108 ? 0.0195 0.0948 0.1188 -0.0339 0.0114  -0.0400 108 THR A CA  
939  C  C   . THR A 108 ? 0.0098 0.1019 0.1071 -0.0184 0.0067  -0.0421 108 THR A C   
940  O  O   . THR A 108 ? 0.0317 0.0958 0.1215 -0.0436 0.0041  -0.0476 108 THR A O   
941  C  CB  . THR A 108 ? 0.0226 0.1198 0.1218 -0.0412 0.0075  -0.0508 108 THR A CB  
942  O  OG1 . THR A 108 ? 0.0392 0.1055 0.1380 -0.0521 -0.0013 -0.0445 108 THR A OG1 
943  C  CG2 . THR A 108 ? 0.0448 0.1204 0.1375 -0.0657 0.0322  -0.0424 108 THR A CG2 
944  N  N   . VAL A 109 ? 0.0204 0.0935 0.1240 -0.0308 0.0122  -0.0500 109 VAL A N   
945  C  CA  . VAL A 109 ? 0.0227 0.1085 0.1394 -0.0399 0.0183  -0.0691 109 VAL A CA  
946  C  C   . VAL A 109 ? 0.0324 0.0990 0.1297 -0.0482 0.0173  -0.0514 109 VAL A C   
947  O  O   . VAL A 109 ? 0.0305 0.1069 0.1518 -0.0458 0.0166  -0.0469 109 VAL A O   
948  C  CB  . VAL A 109 ? 0.0167 0.1294 0.1771 -0.0356 0.0228  -0.0837 109 VAL A CB  
949  C  CG1 . VAL A 109 ? 0.0349 0.1449 0.1846 -0.0359 0.0430  -0.0640 109 VAL A CG1 
950  C  CG2 . VAL A 109 ? 0.0398 0.1351 0.1585 -0.0399 -0.0044 -0.0817 109 VAL A CG2 
951  N  N   . ASP A 110 ? 0.0394 0.1064 0.1299 -0.0474 0.0204  -0.0631 110 ASP A N   
952  C  CA  . ASP A 110 ? 0.0824 0.1173 0.1624 -0.0517 0.0201  -0.0834 110 ASP A CA  
953  C  C   . ASP A 110 ? 0.1003 0.1147 0.1669 -0.0620 0.0212  -0.0851 110 ASP A C   
954  O  O   . ASP A 110 ? 0.1087 0.1258 0.1632 -0.0529 0.0201  -0.0851 110 ASP A O   
955  C  CB  . ASP A 110 ? 0.1165 0.1254 0.1782 -0.0657 0.0630  -0.0934 110 ASP A CB  
956  C  CG  . ASP A 110 ? 0.0797 0.1770 0.1769 -0.0794 0.0589  -0.1046 110 ASP A CG  
957  O  OD1 . ASP A 110 ? 0.1913 0.1679 0.2133 -0.0675 0.0804  -0.0824 110 ASP A OD1 
958  O  OD2 . ASP A 110 ? 0.0775 0.2431 0.2397 -0.0826 0.0570  -0.1089 110 ASP A OD2 
959  N  N   . LYS A 111 ? 0.0317 0.1391 0.1399 -0.0527 0.0052  -0.0665 111 LYS A N   
960  C  CA  . LYS A 111 ? 0.0377 0.1476 0.1820 -0.0596 -0.0100 -0.0500 111 LYS A CA  
961  C  C   . LYS A 111 ? 0.0635 0.1079 0.1370 -0.0525 0.0127  -0.0507 111 LYS A C   
962  O  O   . LYS A 111 ? 0.0633 0.1444 0.1759 -0.0780 0.0185  -0.0413 111 LYS A O   
963  C  CB  . LYS A 111 ? 0.0535 0.1439 0.1861 -0.0754 0.0018  -0.0580 111 LYS A CB  
964  C  CG  . LYS A 111 ? 0.0981 0.1756 0.2349 -0.1147 -0.0114 -0.0438 111 LYS A CG  
965  C  CD  . LYS A 111 ? 0.1965 0.1703 0.2989 -0.0754 -0.0741 -0.0361 111 LYS A CD  
966  C  CE  . LYS A 111 ? 0.2025 0.3687 0.3683 -0.0364 -0.1313 -0.0640 111 LYS A CE  
967  N  NZ  . LYS A 111 ? 0.1188 0.3861 0.4807 -0.0129 0.0194  -0.2224 111 LYS A NZ  
968  N  N   . LYS A 112 ? 0.0538 0.1055 0.1361 -0.0436 0.0150  -0.0675 112 LYS A N   
969  C  CA  . LYS A 112 ? 0.0526 0.0842 0.1449 -0.0463 0.0140  -0.0541 112 LYS A CA  
970  C  C   . LYS A 112 ? 0.0260 0.0985 0.1490 -0.0352 -0.0028 -0.0588 112 LYS A C   
971  O  O   . LYS A 112 ? 0.0288 0.0885 0.1491 -0.0400 0.0120  -0.0595 112 LYS A O   
972  C  CB  . LYS A 112 ? 0.0624 0.0897 0.1796 -0.0256 0.0223  -0.0543 112 LYS A CB  
973  C  CG  . LYS A 112 ? 0.0597 0.1731 0.2070 -0.0274 -0.0030 -0.0168 112 LYS A CG  
974  C  CD  . LYS A 112 ? 0.0615 0.2133 0.2196 -0.0233 -0.0021 -0.0392 112 LYS A CD  
975  C  CE  . LYS A 112 ? 0.1082 0.2395 0.2165 -0.0278 -0.0199 -0.0345 112 LYS A CE  
976  N  NZ  . LYS A 112 ? 0.3449 0.2109 0.2588 -0.1038 -0.0555 -0.0600 112 LYS A NZ  
977  N  N   A LYS A 113 ? 0.0434 0.1150 0.1604 -0.0609 0.0183  -0.0650 113 LYS A N   
978  N  N   B LYS A 113 ? 0.0504 0.1088 0.1593 -0.0617 0.0049  -0.0559 113 LYS A N   
979  C  CA  A LYS A 113 ? 0.0326 0.1165 0.1640 -0.0480 0.0033  -0.0650 113 LYS A CA  
980  C  CA  B LYS A 113 ? 0.0378 0.1067 0.1735 -0.0513 0.0060  -0.0622 113 LYS A CA  
981  C  C   A LYS A 113 ? 0.0239 0.0957 0.1503 -0.0375 0.0094  -0.0568 113 LYS A C   
982  C  C   B LYS A 113 ? 0.0215 0.0981 0.1565 -0.0363 0.0182  -0.0683 113 LYS A C   
983  O  O   A LYS A 113 ? 0.0326 0.0983 0.1615 -0.0482 0.0032  -0.0254 113 LYS A O   
984  O  O   B LYS A 113 ? 0.1271 0.0818 0.2062 -0.0328 0.0166  -0.0666 113 LYS A O   
985  C  CB  A LYS A 113 ? 0.0418 0.1361 0.1817 -0.0626 -0.0021 -0.0539 113 LYS A CB  
986  C  CB  B LYS A 113 ? 0.0460 0.1195 0.1935 -0.0629 0.0057  -0.0595 113 LYS A CB  
987  C  CG  A LYS A 113 ? 0.0286 0.1553 0.1904 -0.0572 0.0104  -0.0455 113 LYS A CG  
988  C  CG  B LYS A 113 ? 0.0459 0.1318 0.2150 -0.0705 0.0111  -0.0227 113 LYS A CG  
989  C  CD  A LYS A 113 ? 0.0231 0.1774 0.1969 -0.0531 -0.0031 -0.0125 113 LYS A CD  
990  C  CD  B LYS A 113 ? 0.0330 0.1453 0.2087 -0.0608 0.0109  -0.0266 113 LYS A CD  
991  C  CE  A LYS A 113 ? 0.0116 0.2141 0.2008 -0.0220 -0.0072 -0.0102 113 LYS A CE  
992  C  CE  B LYS A 113 ? 0.0117 0.1914 0.2262 -0.0272 0.0030  -0.0354 113 LYS A CE  
993  N  NZ  A LYS A 113 ? 0.0378 0.1328 0.2417 -0.0515 -0.0296 -0.0268 113 LYS A NZ  
994  N  NZ  B LYS A 113 ? 0.0110 0.1662 0.2977 -0.0074 0.0369  -0.0348 113 LYS A NZ  
995  N  N   . TYR A 114 ? 0.0191 0.0798 0.1261 -0.0283 0.0083  -0.0527 114 TYR A N   
996  C  CA  . TYR A 114 ? 0.0314 0.0888 0.1350 -0.0374 -0.0012 -0.0566 114 TYR A CA  
997  C  C   . TYR A 114 ? 0.0134 0.0734 0.1335 -0.0208 0.0080  -0.0513 114 TYR A C   
998  O  O   . TYR A 114 ? 0.0175 0.0948 0.1579 -0.0314 0.0190  -0.0508 114 TYR A O   
999  C  CB  . TYR A 114 ? 0.0246 0.1036 0.1469 -0.0413 0.0158  -0.0569 114 TYR A CB  
1000 C  CG  . TYR A 114 ? 0.0227 0.0975 0.1418 -0.0364 0.0076  -0.0528 114 TYR A CG  
1001 C  CD1 . TYR A 114 ? 0.0619 0.0906 0.1550 -0.0517 0.0032  -0.0588 114 TYR A CD1 
1002 C  CD2 . TYR A 114 ? 0.0191 0.1170 0.1771 -0.0374 0.0207  -0.0502 114 TYR A CD2 
1003 C  CE1 . TYR A 114 ? 0.1064 0.1414 0.1703 -0.0458 0.0281  -0.0578 114 TYR A CE1 
1004 C  CE2 . TYR A 114 ? 0.0694 0.1433 0.2027 -0.0356 0.0650  -0.0534 114 TYR A CE2 
1005 C  CZ  . TYR A 114 ? 0.0620 0.1664 0.1872 -0.0395 0.0575  -0.0704 114 TYR A CZ  
1006 O  OH  . TYR A 114 ? 0.1391 0.2746 0.2161 -0.0340 0.0966  -0.0636 114 TYR A OH  
1007 N  N   . ALA A 115 ? 0.0209 0.0850 0.1322 -0.0323 0.0044  -0.0386 115 ALA A N   
1008 C  CA  . ALA A 115 ? 0.0508 0.0697 0.1291 -0.0429 -0.0021 -0.0499 115 ALA A CA  
1009 C  C   . ALA A 115 ? 0.0268 0.0773 0.1308 -0.0346 0.0053  -0.0469 115 ALA A C   
1010 O  O   . ALA A 115 ? 0.0204 0.0975 0.1431 -0.0349 0.0107  -0.0495 115 ALA A O   
1011 C  CB  . ALA A 115 ? 0.0658 0.1008 0.1299 -0.0328 0.0064  -0.0375 115 ALA A CB  
1012 N  N   . ALA A 116 ? 0.0252 0.0788 0.1188 -0.0328 0.0018  -0.0447 116 ALA A N   
1013 C  CA  . ALA A 116 ? 0.0441 0.0913 0.1131 -0.0194 0.0087  -0.0431 116 ALA A CA  
1014 C  C   . ALA A 116 ? 0.0283 0.0829 0.1123 -0.0346 -0.0018 -0.0450 116 ALA A C   
1015 O  O   . ALA A 116 ? 0.0195 0.1025 0.1405 -0.0300 0.0009  -0.0630 116 ALA A O   
1016 C  CB  . ALA A 116 ? 0.0225 0.1091 0.1273 -0.0381 0.0046  -0.0454 116 ALA A CB  
1017 N  N   . GLU A 117 ? 0.0356 0.0915 0.1116 -0.0305 0.0064  -0.0418 117 GLU A N   
1018 C  CA  . GLU A 117 ? 0.0218 0.0825 0.1147 -0.0283 -0.0009 -0.0499 117 GLU A CA  
1019 C  C   . GLU A 117 ? 0.0247 0.0963 0.1116 -0.0325 -0.0022 -0.0539 117 GLU A C   
1020 O  O   . GLU A 117 ? 0.0362 0.1012 0.1299 -0.0439 0.0214  -0.0535 117 GLU A O   
1021 C  CB  . GLU A 117 ? 0.0193 0.1145 0.1188 -0.0369 0.0057  -0.0340 117 GLU A CB  
1022 C  CG  . GLU A 117 ? 0.0243 0.0838 0.1055 -0.0337 0.0059  -0.0454 117 GLU A CG  
1023 C  CD  . GLU A 117 ? 0.0196 0.0715 0.1057 -0.0285 0.0124  -0.0444 117 GLU A CD  
1024 O  OE1 . GLU A 117 ? 0.0263 0.0963 0.1291 -0.0408 0.0094  -0.0475 117 GLU A OE1 
1025 O  OE2 . GLU A 117 ? 0.0278 0.1064 0.0992 -0.0367 -0.0070 -0.0458 117 GLU A OE2 
1026 N  N   . LEU A 118 ? 0.0273 0.0828 0.1203 -0.0316 -0.0080 -0.0440 118 LEU A N   
1027 C  CA  . LEU A 118 ? 0.0331 0.0827 0.1033 -0.0254 -0.0147 -0.0541 118 LEU A CA  
1028 C  C   . LEU A 118 ? 0.0287 0.0991 0.1102 -0.0300 -0.0164 -0.0471 118 LEU A C   
1029 O  O   . LEU A 118 ? 0.0254 0.1102 0.1149 -0.0359 -0.0079 -0.0465 118 LEU A O   
1030 C  CB  . LEU A 118 ? 0.0432 0.0908 0.1346 -0.0264 -0.0336 -0.0561 118 LEU A CB  
1031 C  CG  . LEU A 118 ? 0.0538 0.0987 0.1506 -0.0317 -0.0440 -0.0565 118 LEU A CG  
1032 C  CD1 . LEU A 118 ? 0.0624 0.1432 0.1556 -0.0558 -0.0355 -0.0616 118 LEU A CD1 
1033 C  CD2 . LEU A 118 ? 0.0403 0.1638 0.1602 -0.0403 -0.0439 -0.0480 118 LEU A CD2 
1034 N  N   . HIS A 119 ? 0.0287 0.0955 0.1110 -0.0293 -0.0165 -0.0469 119 HIS A N   
1035 C  CA  . HIS A 119 ? 0.0275 0.0960 0.1060 -0.0312 -0.0065 -0.0559 119 HIS A CA  
1036 C  C   . HIS A 119 ? 0.0289 0.0736 0.1018 -0.0260 -0.0106 -0.0458 119 HIS A C   
1037 O  O   . HIS A 119 ? 0.0518 0.1042 0.1111 -0.0362 -0.0047 -0.0515 119 HIS A O   
1038 C  CB  . HIS A 119 ? 0.0290 0.0940 0.1295 -0.0346 -0.0070 -0.0537 119 HIS A CB  
1039 C  CG  . HIS A 119 ? 0.0248 0.0974 0.1153 -0.0381 0.0073  -0.0509 119 HIS A CG  
1040 N  ND1 . HIS A 119 ? 0.0196 0.0933 0.1095 -0.0331 0.0135  -0.0548 119 HIS A ND1 
1041 C  CD2 . HIS A 119 ? 0.0323 0.0886 0.0987 -0.0422 0.0052  -0.0438 119 HIS A CD2 
1042 C  CE1 . HIS A 119 ? 0.0326 0.0723 0.0974 -0.0250 0.0201  -0.0463 119 HIS A CE1 
1043 N  NE2 . HIS A 119 ? 0.0247 0.0864 0.1177 -0.0359 0.0091  -0.0504 119 HIS A NE2 
1044 N  N   . LEU A 120 ? 0.0362 0.0843 0.1305 -0.0359 -0.0089 -0.0539 120 LEU A N   
1045 C  CA  . LEU A 120 ? 0.0468 0.1082 0.1564 -0.0439 -0.0209 -0.0643 120 LEU A CA  
1046 C  C   . LEU A 120 ? 0.0536 0.1003 0.1730 -0.0591 -0.0029 -0.0542 120 LEU A C   
1047 O  O   . LEU A 120 ? 0.0262 0.1020 0.1589 -0.0391 0.0003  -0.0536 120 LEU A O   
1048 C  CB  . LEU A 120 ? 0.0462 0.1112 0.1955 -0.0491 -0.0343 -0.0413 120 LEU A CB  
1049 C  CG  . LEU A 120 ? 0.0549 0.1098 0.1727 -0.0390 -0.0358 -0.0597 120 LEU A CG  
1050 C  CD1 . LEU A 120 ? 0.1509 0.1680 0.1908 0.0105  0.0384  -0.0223 120 LEU A CD1 
1051 C  CD2 . LEU A 120 ? 0.0851 0.1486 0.1989 -0.0591 -0.0744 -0.0432 120 LEU A CD2 
1052 N  N   . VAL A 121 ? 0.0394 0.0945 0.1448 -0.0397 -0.0181 -0.0502 121 VAL A N   
1053 C  CA  . VAL A 121 ? 0.0439 0.0791 0.1478 -0.0343 -0.0164 -0.0597 121 VAL A CA  
1054 C  C   . VAL A 121 ? 0.0379 0.0858 0.1639 -0.0304 -0.0256 -0.0583 121 VAL A C   
1055 O  O   . VAL A 121 ? 0.1316 0.0990 0.1414 -0.0455 -0.0428 -0.0516 121 VAL A O   
1056 C  CB  . VAL A 121 ? 0.0746 0.0958 0.1346 -0.0376 0.0032  -0.0465 121 VAL A CB  
1057 C  CG1 . VAL A 121 ? 0.0499 0.1021 0.1502 -0.0331 -0.0103 -0.0500 121 VAL A CG1 
1058 C  CG2 . VAL A 121 ? 0.0832 0.0895 0.1429 -0.0384 0.0225  -0.0504 121 VAL A CG2 
1059 N  N   . HIS A 122 ? 0.0230 0.0848 0.1430 -0.0263 -0.0140 -0.0454 122 HIS A N   
1060 C  CA  . HIS A 122 ? 0.0514 0.0878 0.1441 -0.0418 -0.0206 -0.0545 122 HIS A CA  
1061 C  C   . HIS A 122 ? 0.0315 0.1017 0.1326 -0.0348 -0.0135 -0.0562 122 HIS A C   
1062 O  O   . HIS A 122 ? 0.0398 0.0872 0.1499 -0.0358 -0.0212 -0.0517 122 HIS A O   
1063 C  CB  . HIS A 122 ? 0.0586 0.0841 0.1936 -0.0523 -0.0089 -0.0597 122 HIS A CB  
1064 C  CG  . HIS A 122 ? 0.0439 0.0937 0.2087 -0.0407 -0.0294 -0.0562 122 HIS A CG  
1065 N  ND1 . HIS A 122 ? 0.0444 0.0806 0.1840 -0.0401 -0.0219 -0.0495 122 HIS A ND1 
1066 C  CD2 . HIS A 122 ? 0.0350 0.1166 0.1940 -0.0410 -0.0252 -0.0564 122 HIS A CD2 
1067 C  CE1 . HIS A 122 ? 0.0305 0.1161 0.1698 -0.0454 -0.0164 -0.0299 122 HIS A CE1 
1068 N  NE2 . HIS A 122 ? 0.0239 0.1221 0.1947 -0.0293 -0.0265 -0.0558 122 HIS A NE2 
1069 N  N   . TRP A 123 ? 0.0425 0.0883 0.1439 -0.0302 -0.0065 -0.0527 123 TRP A N   
1070 C  CA  . TRP A 123 ? 0.0323 0.0958 0.1455 -0.0457 0.0062  -0.0460 123 TRP A CA  
1071 C  C   . TRP A 123 ? 0.0405 0.0977 0.1786 -0.0512 -0.0080 -0.0372 123 TRP A C   
1072 O  O   . TRP A 123 ? 0.0326 0.1296 0.2056 -0.0523 -0.0069 -0.0482 123 TRP A O   
1073 C  CB  . TRP A 123 ? 0.0671 0.1203 0.1641 -0.0262 0.0268  -0.0465 123 TRP A CB  
1074 C  CG  . TRP A 123 ? 0.1338 0.1000 0.2070 0.0002  -0.0142 -0.0665 123 TRP A CG  
1075 C  CD1 . TRP A 123 ? 0.2772 0.1296 0.1819 0.0587  -0.0124 -0.0846 123 TRP A CD1 
1076 C  CD2 . TRP A 123 ? 0.1624 0.1012 0.1804 -0.0083 -0.0146 -0.0607 123 TRP A CD2 
1077 N  NE1 . TRP A 123 ? 0.3035 0.1174 0.2284 0.0190  -0.0406 -0.0655 123 TRP A NE1 
1078 C  CE2 . TRP A 123 ? 0.2511 0.1302 0.2001 0.0119  -0.0370 -0.0716 123 TRP A CE2 
1079 C  CE3 . TRP A 123 ? 0.0944 0.1313 0.2022 0.0124  0.0020  -0.0453 123 TRP A CE3 
1080 C  CZ2 . TRP A 123 ? 0.1433 0.1779 0.2474 -0.0285 -0.0792 -0.0767 123 TRP A CZ2 
1081 C  CZ3 . TRP A 123 ? 0.1363 0.1298 0.2645 0.0298  -0.0420 -0.0696 123 TRP A CZ3 
1082 C  CH2 . TRP A 123 ? 0.1841 0.1603 0.2780 0.0156  -0.0699 -0.0608 123 TRP A CH2 
1083 N  N   . ASN A 124 ? 0.0268 0.0959 0.1565 -0.0414 0.0010  -0.0310 124 ASN A N   
1084 C  CA  . ASN A 124 ? 0.0388 0.0904 0.1614 -0.0468 -0.0037 -0.0295 124 ASN A CA  
1085 C  C   . ASN A 124 ? 0.0267 0.0925 0.1850 -0.0417 0.0072  -0.0249 124 ASN A C   
1086 O  O   . ASN A 124 ? 0.0237 0.1068 0.1647 -0.0346 0.0024  -0.0374 124 ASN A O   
1087 C  CB  . ASN A 124 ? 0.0493 0.1283 0.1595 -0.0394 -0.0002 -0.0075 124 ASN A CB  
1088 C  CG  . ASN A 124 ? 0.0393 0.0980 0.1976 -0.0495 0.0085  -0.0222 124 ASN A CG  
1089 O  OD1 . ASN A 124 ? 0.0374 0.1216 0.2168 -0.0595 0.0184  -0.0248 124 ASN A OD1 
1090 N  ND2 . ASN A 124 ? 0.0784 0.1210 0.1868 -0.0420 0.0172  -0.0241 124 ASN A ND2 
1091 N  N   . THR A 125 ? 0.0485 0.1026 0.2258 -0.0612 -0.0089 -0.0264 125 THR A N   
1092 C  CA  . THR A 125 ? 0.0723 0.1057 0.2488 -0.0661 -0.0361 -0.0494 125 THR A CA  
1093 C  C   . THR A 125 ? 0.0492 0.1266 0.2889 -0.0672 -0.0118 -0.0452 125 THR A C   
1094 O  O   . THR A 125 ? 0.0675 0.1134 0.3139 -0.0612 -0.0499 -0.0607 125 THR A O   
1095 C  CB  . THR A 125 ? 0.0939 0.1742 0.3212 -0.0262 -0.1002 -0.0798 125 THR A CB  
1096 O  OG1 . THR A 125 ? 0.1459 0.2432 0.4653 -0.0272 0.0157  -0.0752 125 THR A OG1 
1097 C  CG2 . THR A 125 ? 0.1018 0.2202 0.3361 -0.0564 -0.1252 -0.0548 125 THR A CG2 
1098 N  N   . LYS A 126 ? 0.0467 0.1144 0.2624 -0.0658 0.0076  -0.0001 126 LYS A N   
1099 C  CA  . LYS A 126 ? 0.0712 0.1323 0.2933 -0.0623 0.0134  0.0190  126 LYS A CA  
1100 C  C   . LYS A 126 ? 0.1001 0.1342 0.2540 -0.0266 0.0133  -0.0012 126 LYS A C   
1101 O  O   . LYS A 126 ? 0.1021 0.1071 0.4044 -0.0340 -0.0255 -0.0013 126 LYS A O   
1102 C  CB  . LYS A 126 ? 0.1393 0.1802 0.2992 -0.0379 -0.0270 0.0318  126 LYS A CB  
1103 C  CG  . LYS A 126 ? 0.1064 0.1775 0.3339 -0.0486 0.0024  0.0196  126 LYS A CG  
1104 C  CD  . LYS A 126 ? 0.2909 0.3696 0.3685 0.0057  0.1305  -0.0550 126 LYS A CD  
1105 C  CE  . LYS A 126 ? 0.2623 0.3279 0.6646 -0.1267 -0.0030 0.0947  126 LYS A CE  
1106 N  NZ  . LYS A 126 ? 0.1938 0.6172 0.6265 0.0983  0.1806  0.1571  126 LYS A NZ  
1107 N  N   . TYR A 127 ? 0.0658 0.0892 0.2159 -0.0392 -0.0044 -0.0381 127 TYR A N   
1108 C  CA  . TYR A 127 ? 0.0491 0.1051 0.2072 -0.0469 -0.0211 -0.0487 127 TYR A CA  
1109 C  C   . TYR A 127 ? 0.0411 0.1073 0.2100 -0.0463 0.0082  -0.0251 127 TYR A C   
1110 O  O   . TYR A 127 ? 0.0271 0.1473 0.2232 -0.0214 -0.0188 -0.0434 127 TYR A O   
1111 C  CB  . TYR A 127 ? 0.0529 0.1134 0.2277 -0.0591 -0.0265 -0.0332 127 TYR A CB  
1112 C  CG  . TYR A 127 ? 0.0628 0.1285 0.2149 -0.0392 -0.0388 -0.0317 127 TYR A CG  
1113 C  CD1 . TYR A 127 ? 0.0719 0.1376 0.1931 -0.0414 -0.0156 -0.0303 127 TYR A CD1 
1114 C  CD2 . TYR A 127 ? 0.0403 0.1143 0.1843 -0.0414 0.0099  -0.0140 127 TYR A CD2 
1115 C  CE1 . TYR A 127 ? 0.1091 0.1364 0.1929 -0.0447 -0.0074 -0.0096 127 TYR A CE1 
1116 C  CE2 . TYR A 127 ? 0.0848 0.1285 0.1838 -0.0603 -0.0089 -0.0168 127 TYR A CE2 
1117 C  CZ  . TYR A 127 ? 0.0655 0.1484 0.1938 -0.0485 -0.0026 -0.0187 127 TYR A CZ  
1118 O  OH  . TYR A 127 ? 0.1625 0.1835 0.1920 -0.0656 -0.0059 -0.0126 127 TYR A OH  
1119 N  N   . GLY A 128 ? 0.0547 0.1304 0.2204 -0.0345 -0.0075 -0.0445 128 GLY A N   
1120 C  CA  . GLY A 128 ? 0.0709 0.1302 0.2286 -0.0374 -0.0059 -0.0639 128 GLY A CA  
1121 C  C   . GLY A 128 ? 0.1129 0.0881 0.1965 -0.0329 -0.0254 -0.0832 128 GLY A C   
1122 O  O   . GLY A 128 ? 0.0927 0.1339 0.2325 -0.0388 -0.0569 -0.0815 128 GLY A O   
1123 N  N   . ASP A 129 ? 0.0956 0.1015 0.1817 -0.0325 -0.0288 -0.0586 129 ASP A N   
1124 C  CA  . ASP A 129 ? 0.1392 0.1238 0.1816 -0.0337 -0.0276 -0.0570 129 ASP A CA  
1125 C  C   . ASP A 129 ? 0.0559 0.1292 0.1559 -0.0256 -0.0071 -0.0446 129 ASP A C   
1126 O  O   . ASP A 129 ? 0.1279 0.1139 0.1668 -0.0337 -0.0265 -0.0332 129 ASP A O   
1127 C  CB  . ASP A 129 ? 0.1046 0.1133 0.1867 -0.0547 -0.0190 -0.0627 129 ASP A CB  
1128 C  CG  . ASP A 129 ? 0.0829 0.1450 0.2622 -0.0543 0.0080  0.0062  129 ASP A CG  
1129 O  OD1 . ASP A 129 ? 0.1775 0.1338 0.3005 -0.0568 -0.0245 -0.0867 129 ASP A OD1 
1130 O  OD2 . ASP A 129 ? 0.1194 0.1701 0.3780 -0.0322 -0.0278 -0.0636 129 ASP A OD2 
1131 N  N   A VAL A 130 ? 0.1194 0.1060 0.1428 -0.0381 -0.0275 -0.0575 130 VAL A N   
1132 N  N   B VAL A 130 ? 0.1626 0.1322 0.1543 -0.0292 -0.0036 -0.0452 130 VAL A N   
1133 C  CA  A VAL A 130 ? 0.1194 0.1213 0.1740 -0.0681 -0.0332 -0.0557 130 VAL A CA  
1134 C  CA  B VAL A 130 ? 0.1564 0.1525 0.2043 -0.0504 -0.0019 -0.0598 130 VAL A CA  
1135 C  C   A VAL A 130 ? 0.1037 0.0773 0.1619 -0.0535 0.0065  -0.0545 130 VAL A C   
1136 C  C   B VAL A 130 ? 0.1316 0.1731 0.1570 -0.0308 0.0565  -0.0350 130 VAL A C   
1137 O  O   A VAL A 130 ? 0.0778 0.0606 0.1070 -0.0573 0.0181  -0.0216 130 VAL A O   
1138 O  O   B VAL A 130 ? 0.0533 0.1407 0.1319 -0.0354 0.0709  -0.0207 130 VAL A O   
1139 C  CB  A VAL A 130 ? 0.0854 0.1095 0.1936 -0.0759 -0.0284 -0.0460 130 VAL A CB  
1140 C  CB  B VAL A 130 ? 0.1658 0.1552 0.2405 -0.0339 0.0411  -0.0369 130 VAL A CB  
1141 C  CG1 A VAL A 130 ? 0.1643 0.1053 0.1649 -0.0120 -0.0168 -0.0471 130 VAL A CG1 
1142 C  CG1 B VAL A 130 ? 0.0861 0.1557 0.3080 -0.0635 0.0502  0.0390  130 VAL A CG1 
1143 C  CG2 A VAL A 130 ? 0.0674 0.1188 0.1835 -0.0578 -0.0483 -0.0438 130 VAL A CG2 
1144 C  CG2 B VAL A 130 ? 0.1700 0.1772 0.2897 0.0200  0.0966  -0.0579 130 VAL A CG2 
1145 N  N   . GLY A 131 ? 0.1560 0.1488 0.1573 0.0008  0.0185  -0.0565 131 GLY A N   
1146 C  CA  . GLY A 131 ? 0.1497 0.1540 0.1720 -0.0013 -0.0049 -0.0487 131 GLY A CA  
1147 C  C   . GLY A 131 ? 0.0414 0.1577 0.1620 -0.0171 0.0203  -0.0456 131 GLY A C   
1148 O  O   . GLY A 131 ? 0.0818 0.1383 0.1728 -0.0222 0.0069  -0.0491 131 GLY A O   
1149 N  N   . LYS A 132 ? 0.0836 0.1107 0.1726 -0.0285 0.0126  -0.0688 132 LYS A N   
1150 C  CA  . LYS A 132 ? 0.0486 0.1316 0.1683 -0.0285 0.0048  -0.0621 132 LYS A CA  
1151 C  C   . LYS A 132 ? 0.0514 0.1080 0.1472 -0.0284 -0.0074 -0.0383 132 LYS A C   
1152 O  O   . LYS A 132 ? 0.0457 0.1014 0.1655 -0.0247 -0.0185 -0.0474 132 LYS A O   
1153 C  CB  . LYS A 132 ? 0.0411 0.1307 0.1784 -0.0409 -0.0193 -0.0460 132 LYS A CB  
1154 C  CG  . LYS A 132 ? 0.1345 0.1406 0.2865 -0.0284 -0.0258 -0.0791 132 LYS A CG  
1155 C  CD  . LYS A 132 ? 0.1075 0.1679 0.3884 -0.0053 -0.0247 -0.0893 132 LYS A CD  
1156 C  CE  . LYS A 132 ? 0.2037 0.1924 0.5345 -0.0060 -0.1576 -0.2042 132 LYS A CE  
1157 N  NZ  . LYS A 132 ? 0.1600 0.7656 0.5447 0.0611  -0.0646 0.0466  132 LYS A NZ  
1158 N  N   . ALA A 133 ? 0.0387 0.0969 0.1617 -0.0308 0.0084  -0.0400 133 ALA A N   
1159 C  CA  . ALA A 133 ? 0.0243 0.1304 0.1421 -0.0264 0.0055  -0.0466 133 ALA A CA  
1160 C  C   . ALA A 133 ? 0.0441 0.1005 0.1429 -0.0156 0.0124  -0.0477 133 ALA A C   
1161 O  O   . ALA A 133 ? 0.0160 0.1283 0.1527 -0.0334 0.0076  -0.0557 133 ALA A O   
1162 C  CB  . ALA A 133 ? 0.0351 0.1095 0.1535 -0.0298 -0.0103 -0.0475 133 ALA A CB  
1163 N  N   . LEU A 134 ? 0.0485 0.0884 0.1548 -0.0311 0.0098  -0.0439 134 LEU A N   
1164 C  CA  . LEU A 134 ? 0.0269 0.1070 0.1574 -0.0260 0.0124  -0.0545 134 LEU A CA  
1165 C  C   . LEU A 134 ? 0.0175 0.1297 0.1784 -0.0370 0.0134  -0.0366 134 LEU A C   
1166 O  O   . LEU A 134 ? 0.0344 0.1328 0.1834 -0.0574 0.0039  -0.0392 134 LEU A O   
1167 C  CB  . LEU A 134 ? 0.0757 0.1177 0.1631 -0.0230 0.0381  -0.0471 134 LEU A CB  
1168 C  CG  . LEU A 134 ? 0.1209 0.1377 0.1811 -0.0374 0.0137  -0.0355 134 LEU A CG  
1169 C  CD1 . LEU A 134 ? 0.2343 0.1824 0.2526 -0.0256 0.1091  -0.0511 134 LEU A CD1 
1170 C  CD2 . LEU A 134 ? 0.1143 0.1479 0.2225 -0.0205 0.0314  -0.0431 134 LEU A CD2 
1171 N  N   . GLN A 135 ? 0.0119 0.1281 0.1611 -0.0260 0.0063  -0.0352 135 GLN A N   
1172 C  CA  . GLN A 135 ? 0.0671 0.1443 0.1518 -0.0240 -0.0068 -0.0505 135 GLN A CA  
1173 C  C   . GLN A 135 ? 0.0457 0.1233 0.1540 -0.0139 0.0094  -0.0357 135 GLN A C   
1174 O  O   . GLN A 135 ? 0.0477 0.1958 0.1828 -0.0058 0.0055  -0.0146 135 GLN A O   
1175 C  CB  . GLN A 135 ? 0.0330 0.1509 0.1935 -0.0195 0.0033  -0.0546 135 GLN A CB  
1176 C  CG  . GLN A 135 ? 0.0761 0.2168 0.2035 0.0027  0.0162  -0.0686 135 GLN A CG  
1177 C  CD  . GLN A 135 ? 0.1694 0.2967 0.3027 0.0829  0.0108  -0.1147 135 GLN A CD  
1178 O  OE1 . GLN A 135 ? 0.2295 0.3853 0.3861 0.1449  -0.0559 -0.1399 135 GLN A OE1 
1179 N  NE2 . GLN A 135 ? 0.0831 0.3201 0.4767 -0.0157 0.0229  -0.1655 135 GLN A NE2 
1180 N  N   A GLN A 136 ? 0.0306 0.1150 0.1626 -0.0497 0.0106  -0.0535 136 GLN A N   
1181 N  N   B GLN A 136 ? 0.0309 0.1157 0.1684 -0.0501 0.0111  -0.0553 136 GLN A N   
1182 C  CA  A GLN A 136 ? 0.0247 0.1339 0.1459 -0.0320 0.0030  -0.0467 136 GLN A CA  
1183 C  CA  B GLN A 136 ? 0.0336 0.1324 0.1509 -0.0389 0.0044  -0.0416 136 GLN A CA  
1184 C  C   A GLN A 136 ? 0.0245 0.1274 0.1529 -0.0465 0.0189  -0.0344 136 GLN A C   
1185 C  C   B GLN A 136 ? 0.0282 0.1314 0.1541 -0.0520 0.0186  -0.0333 136 GLN A C   
1186 O  O   A GLN A 136 ? 0.0199 0.1217 0.1630 -0.0394 0.0114  -0.0441 136 GLN A O   
1187 O  O   B GLN A 136 ? 0.0250 0.1441 0.1821 -0.0490 -0.0026 -0.0319 136 GLN A O   
1188 C  CB  A GLN A 136 ? 0.0369 0.1312 0.1608 -0.0445 0.0153  -0.0485 136 GLN A CB  
1189 C  CB  B GLN A 136 ? 0.0732 0.1335 0.1757 -0.0647 0.0031  -0.0559 136 GLN A CB  
1190 C  CG  A GLN A 136 ? 0.0972 0.1448 0.1810 0.0019  0.0042  -0.0600 136 GLN A CG  
1191 C  CG  B GLN A 136 ? 0.0608 0.1209 0.2667 -0.0656 -0.0313 -0.0551 136 GLN A CG  
1192 C  CD  A GLN A 136 ? 0.0394 0.1165 0.1480 -0.0411 0.0447  -0.0260 136 GLN A CD  
1193 C  CD  B GLN A 136 ? 0.0913 0.1766 0.2424 -0.0832 0.0050  -0.0196 136 GLN A CD  
1194 O  OE1 A GLN A 136 ? 0.1082 0.1477 0.1434 0.0046  0.0634  -0.0047 136 GLN A OE1 
1195 O  OE1 B GLN A 136 ? 0.1844 0.2280 0.2249 -0.0534 0.0280  0.0300  136 GLN A OE1 
1196 N  NE2 A GLN A 136 ? 0.1427 0.1575 0.1563 0.0269  0.0331  -0.0614 136 GLN A NE2 
1197 N  NE2 B GLN A 136 ? 0.2173 0.1830 0.2791 0.0242  -0.0671 0.0042  136 GLN A NE2 
1198 N  N   . PRO A 137 ? 0.0179 0.1184 0.1483 -0.0359 0.0124  -0.0241 137 PRO A N   
1199 C  CA  . PRO A 137 ? 0.0275 0.1168 0.1415 -0.0417 -0.0019 -0.0336 137 PRO A CA  
1200 C  C   . PRO A 137 ? 0.0187 0.1279 0.1487 -0.0326 0.0214  -0.0474 137 PRO A C   
1201 O  O   . PRO A 137 ? 0.0536 0.1350 0.2095 -0.0273 -0.0079 -0.0561 137 PRO A O   
1202 C  CB  . PRO A 137 ? 0.0563 0.1542 0.1524 -0.0312 0.0106  -0.0316 137 PRO A CB  
1203 C  CG  . PRO A 137 ? 0.1432 0.1625 0.1868 -0.0259 -0.0006 -0.0488 137 PRO A CG  
1204 C  CD  . PRO A 137 ? 0.0761 0.1593 0.1671 -0.0217 0.0073  -0.0172 137 PRO A CD  
1205 N  N   . ASP A 138 ? 0.0192 0.1183 0.1537 -0.0216 0.0040  -0.0449 138 ASP A N   
1206 C  CA  . ASP A 138 ? 0.0110 0.1842 0.1602 -0.0241 0.0198  -0.0411 138 ASP A CA  
1207 C  C   . ASP A 138 ? 0.0168 0.1233 0.1549 -0.0348 0.0111  -0.0423 138 ASP A C   
1208 O  O   . ASP A 138 ? 0.0212 0.1431 0.1894 -0.0448 0.0099  -0.0463 138 ASP A O   
1209 C  CB  . ASP A 138 ? 0.0550 0.1869 0.1563 -0.0519 0.0143  -0.0262 138 ASP A CB  
1210 C  CG  . ASP A 138 ? 0.0302 0.1977 0.2119 -0.0672 0.0212  -0.0414 138 ASP A CG  
1211 O  OD1 . ASP A 138 ? 0.0644 0.1752 0.1949 -0.0447 0.0282  -0.0257 138 ASP A OD1 
1212 O  OD2 . ASP A 138 ? 0.1064 0.2431 0.2192 -0.1059 0.0425  0.0068  138 ASP A OD2 
1213 N  N   . GLY A 139 ? 0.0172 0.1102 0.1357 -0.0334 0.0059  -0.0296 139 GLY A N   
1214 C  CA  . GLY A 139 ? 0.0279 0.1113 0.1403 -0.0447 -0.0020 -0.0354 139 GLY A CA  
1215 C  C   . GLY A 139 ? 0.0160 0.0964 0.1278 -0.0291 0.0114  -0.0499 139 GLY A C   
1216 O  O   . GLY A 139 ? 0.0268 0.1027 0.1471 -0.0406 -0.0032 -0.0401 139 GLY A O   
1217 N  N   A LEU A 140 ? 0.0247 0.1077 0.1696 -0.0430 0.0159  -0.0506 140 LEU A N   
1218 N  N   B LEU A 140 ? 0.0258 0.1086 0.1735 -0.0439 0.0116  -0.0480 140 LEU A N   
1219 C  CA  A LEU A 140 ? 0.0310 0.1021 0.1543 -0.0479 0.0175  -0.0543 140 LEU A CA  
1220 C  CA  B LEU A 140 ? 0.0311 0.1023 0.1551 -0.0480 0.0174  -0.0525 140 LEU A CA  
1221 C  C   A LEU A 140 ? 0.0231 0.0959 0.1353 -0.0387 0.0143  -0.0351 140 LEU A C   
1222 C  C   B LEU A 140 ? 0.0236 0.0974 0.1341 -0.0394 0.0111  -0.0372 140 LEU A C   
1223 O  O   A LEU A 140 ? 0.0240 0.1133 0.1408 -0.0434 0.0215  -0.0478 140 LEU A O   
1224 O  O   B LEU A 140 ? 0.0201 0.1161 0.1380 -0.0390 0.0190  -0.0520 140 LEU A O   
1225 C  CB  A LEU A 140 ? 0.0424 0.1296 0.1726 -0.0662 0.0181  -0.0489 140 LEU A CB  
1226 C  CB  B LEU A 140 ? 0.0425 0.1303 0.1647 -0.0668 0.0230  -0.0538 140 LEU A CB  
1227 C  CG  A LEU A 140 ? 0.0286 0.1775 0.2180 -0.0610 0.0315  -0.0613 140 LEU A CG  
1228 C  CG  B LEU A 140 ? 0.0283 0.1669 0.2007 -0.0579 0.0315  -0.0494 140 LEU A CG  
1229 C  CD1 A LEU A 140 ? 0.0681 0.1495 0.2234 -0.0886 0.0656  -0.0461 140 LEU A CD1 
1230 C  CD1 B LEU A 140 ? 0.0593 0.1852 0.2191 -0.0963 0.0410  -0.0496 140 LEU A CD1 
1231 C  CD2 A LEU A 140 ? 0.0370 0.1797 0.2031 -0.0727 0.0129  -0.0413 140 LEU A CD2 
1232 C  CD2 B LEU A 140 ? 0.0577 0.1643 0.1856 -0.0775 0.0280  -0.0584 140 LEU A CD2 
1233 N  N   . ALA A 141 ? 0.0200 0.0809 0.1553 -0.0307 0.0069  -0.0450 141 ALA A N   
1234 C  CA  . ALA A 141 ? 0.0136 0.1111 0.1427 -0.0267 0.0080  -0.0578 141 ALA A CA  
1235 C  C   . ALA A 141 ? 0.0161 0.0960 0.1345 -0.0295 0.0184  -0.0604 141 ALA A C   
1236 O  O   . ALA A 141 ? 0.0299 0.0976 0.1365 -0.0369 -0.0080 -0.0526 141 ALA A O   
1237 C  CB  . ALA A 141 ? 0.0170 0.1305 0.1645 -0.0360 0.0111  -0.0569 141 ALA A CB  
1238 N  N   . VAL A 142 ? 0.0174 0.0913 0.1324 -0.0256 -0.0032 -0.0489 142 VAL A N   
1239 C  CA  . VAL A 142 ? 0.0221 0.1003 0.1282 -0.0338 0.0037  -0.0584 142 VAL A CA  
1240 C  C   . VAL A 142 ? 0.0196 0.0963 0.1231 -0.0340 0.0099  -0.0445 142 VAL A C   
1241 O  O   . VAL A 142 ? 0.0308 0.0947 0.1199 -0.0457 0.0136  -0.0426 142 VAL A O   
1242 C  CB  . VAL A 142 ? 0.0296 0.1013 0.1325 -0.0450 0.0079  -0.0462 142 VAL A CB  
1243 C  CG1 . VAL A 142 ? 0.0353 0.1234 0.1292 -0.0439 -0.0012 -0.0347 142 VAL A CG1 
1244 C  CG2 . VAL A 142 ? 0.0229 0.1476 0.1670 -0.0472 0.0185  -0.0824 142 VAL A CG2 
1245 N  N   . LEU A 143 ? 0.0249 0.0783 0.1346 -0.0321 0.0000  -0.0457 143 LEU A N   
1246 C  CA  . LEU A 143 ? 0.0208 0.0906 0.1443 -0.0329 0.0046  -0.0456 143 LEU A CA  
1247 C  C   . LEU A 143 ? 0.0174 0.0793 0.1198 -0.0163 -0.0183 -0.0373 143 LEU A C   
1248 O  O   . LEU A 143 ? 0.0270 0.0791 0.1328 -0.0326 -0.0072 -0.0398 143 LEU A O   
1249 C  CB  . LEU A 143 ? 0.0301 0.1103 0.1628 -0.0447 -0.0066 -0.0424 143 LEU A CB  
1250 C  CG  . LEU A 143 ? 0.0254 0.1408 0.2110 -0.0300 -0.0326 -0.0622 143 LEU A CG  
1251 C  CD1 . LEU A 143 ? 0.0107 0.1668 0.2166 -0.0256 0.0031  -0.0627 143 LEU A CD1 
1252 C  CD2 . LEU A 143 ? 0.0311 0.1626 0.2469 -0.0423 -0.0401 -0.0523 143 LEU A CD2 
1253 N  N   . GLY A 144 ? 0.0218 0.0718 0.1537 -0.0303 0.0071  -0.0444 144 GLY A N   
1254 C  CA  . GLY A 144 ? 0.0268 0.0790 0.1251 -0.0347 0.0080  -0.0534 144 GLY A CA  
1255 C  C   . GLY A 144 ? 0.0297 0.0917 0.1256 -0.0377 0.0031  -0.0589 144 GLY A C   
1256 O  O   . GLY A 144 ? 0.0199 0.0994 0.1159 -0.0315 0.0036  -0.0483 144 GLY A O   
1257 N  N   . ILE A 145 ? 0.0244 0.0850 0.1212 -0.0318 0.0003  -0.0511 145 ILE A N   
1258 C  CA  . ILE A 145 ? 0.0269 0.0876 0.1402 -0.0321 -0.0070 -0.0530 145 ILE A CA  
1259 C  C   . ILE A 145 ? 0.0214 0.0923 0.1373 -0.0315 0.0002  -0.0512 145 ILE A C   
1260 O  O   . ILE A 145 ? 0.0297 0.0962 0.1279 -0.0373 -0.0084 -0.0461 145 ILE A O   
1261 C  CB  . ILE A 145 ? 0.0385 0.1080 0.1719 -0.0460 -0.0201 -0.0450 145 ILE A CB  
1262 C  CG1 . ILE A 145 ? 0.0719 0.1347 0.2343 -0.0708 -0.0634 -0.0244 145 ILE A CG1 
1263 C  CG2 . ILE A 145 ? 0.0556 0.1037 0.1802 -0.0520 -0.0355 -0.0391 145 ILE A CG2 
1264 C  CD1 . ILE A 145 ? 0.0615 0.1455 0.2359 -0.0548 -0.0638 -0.0514 145 ILE A CD1 
1265 N  N   . PHE A 146 ? 0.0192 0.0955 0.1132 -0.0321 0.0042  -0.0406 146 PHE A N   
1266 C  CA  . PHE A 146 ? 0.0227 0.0985 0.1249 -0.0389 0.0156  -0.0383 146 PHE A CA  
1267 C  C   . PHE A 146 ? 0.0131 0.0748 0.1434 -0.0211 0.0080  -0.0417 146 PHE A C   
1268 O  O   . PHE A 146 ? 0.0154 0.1143 0.1630 -0.0303 0.0031  -0.0429 146 PHE A O   
1269 C  CB  . PHE A 146 ? 0.0129 0.0979 0.1251 -0.0245 0.0115  -0.0422 146 PHE A CB  
1270 C  CG  . PHE A 146 ? 0.0248 0.0850 0.1194 -0.0373 0.0148  -0.0477 146 PHE A CG  
1271 C  CD1 . PHE A 146 ? 0.0220 0.1131 0.1186 -0.0407 0.0115  -0.0380 146 PHE A CD1 
1272 C  CD2 . PHE A 146 ? 0.0221 0.0914 0.1124 -0.0301 0.0131  -0.0760 146 PHE A CD2 
1273 C  CE1 . PHE A 146 ? 0.0360 0.0775 0.1140 -0.0268 0.0025  -0.0438 146 PHE A CE1 
1274 C  CE2 . PHE A 146 ? 0.0202 0.1133 0.1273 -0.0380 0.0233  -0.0499 146 PHE A CE2 
1275 C  CZ  . PHE A 146 ? 0.0275 0.0983 0.1324 -0.0414 0.0160  -0.0666 146 PHE A CZ  
1276 N  N   . LEU A 147 ? 0.0392 0.0861 0.1164 -0.0325 0.0034  -0.0429 147 LEU A N   
1277 C  CA  . LEU A 147 ? 0.0259 0.0978 0.1371 -0.0380 -0.0033 -0.0411 147 LEU A CA  
1278 C  C   . LEU A 147 ? 0.0262 0.0889 0.1417 -0.0364 -0.0014 -0.0431 147 LEU A C   
1279 O  O   . LEU A 147 ? 0.0260 0.0972 0.1609 -0.0368 -0.0027 -0.0530 147 LEU A O   
1280 C  CB  . LEU A 147 ? 0.0610 0.0969 0.1339 -0.0259 0.0013  -0.0493 147 LEU A CB  
1281 C  CG  . LEU A 147 ? 0.0958 0.1100 0.1470 -0.0291 -0.0242 -0.0539 147 LEU A CG  
1282 C  CD1 . LEU A 147 ? 0.0512 0.0945 0.1578 -0.0343 -0.0267 -0.0664 147 LEU A CD1 
1283 C  CD2 . LEU A 147 ? 0.0339 0.1346 0.1538 -0.0424 -0.0173 -0.0597 147 LEU A CD2 
1284 N  N   . LYS A 148 ? 0.0179 0.0969 0.1511 -0.0297 -0.0018 -0.0348 148 LYS A N   
1285 C  CA  . LYS A 148 ? 0.0237 0.0967 0.1613 -0.0370 0.0059  -0.0541 148 LYS A CA  
1286 C  C   . LYS A 148 ? 0.0253 0.1108 0.1606 -0.0441 0.0118  -0.0429 148 LYS A C   
1287 O  O   . LYS A 148 ? 0.0576 0.1261 0.1763 -0.0710 -0.0169 -0.0354 148 LYS A O   
1288 C  CB  . LYS A 148 ? 0.0416 0.1382 0.1758 -0.0341 0.0158  -0.0554 148 LYS A CB  
1289 C  CG  . LYS A 148 ? 0.0393 0.1661 0.1917 -0.0277 0.0439  -0.0525 148 LYS A CG  
1290 C  CD  . LYS A 148 ? 0.1200 0.1923 0.2190 -0.0458 0.0809  -0.0719 148 LYS A CD  
1291 C  CE  . LYS A 148 ? 0.1605 0.4056 0.3143 0.0394  0.1188  -0.0580 148 LYS A CE  
1292 N  NZ  . LYS A 148 ? 0.2751 0.5319 0.4282 0.0474  0.1067  -0.1815 148 LYS A NZ  
1293 N  N   . VAL A 149 ? 0.0554 0.0780 0.1698 -0.0441 -0.0150 -0.0353 149 VAL A N   
1294 C  CA  . VAL A 149 ? 0.0644 0.0973 0.1843 -0.0422 0.0015  -0.0410 149 VAL A CA  
1295 C  C   . VAL A 149 ? 0.0559 0.1026 0.1826 -0.0557 0.0062  -0.0390 149 VAL A C   
1296 O  O   . VAL A 149 ? 0.0956 0.1280 0.2000 -0.0280 -0.0154 -0.0573 149 VAL A O   
1297 C  CB  . VAL A 149 ? 0.0623 0.1286 0.1945 -0.0365 -0.0004 -0.0222 149 VAL A CB  
1298 C  CG1 . VAL A 149 ? 0.0994 0.2226 0.2115 -0.0064 -0.0049 0.0061  149 VAL A CG1 
1299 C  CG2 . VAL A 149 ? 0.0800 0.1685 0.2024 -0.0157 0.0334  -0.0245 149 VAL A CG2 
1300 N  N   . GLY A 150 ? 0.0497 0.1293 0.1892 -0.0212 -0.0108 -0.0515 150 GLY A N   
1301 C  CA  . GLY A 150 ? 0.0493 0.2081 0.2336 0.0081  -0.0085 -0.0717 150 GLY A CA  
1302 C  C   . GLY A 150 ? 0.0864 0.1458 0.2088 -0.0055 -0.0160 -0.0189 150 GLY A C   
1303 O  O   . GLY A 150 ? 0.0746 0.1511 0.2143 -0.0158 -0.0041 -0.0302 150 GLY A O   
1304 N  N   A SER A 151 ? 0.0730 0.1588 0.2090 -0.0053 -0.0359 -0.0528 151 SER A N   
1305 N  N   B SER A 151 ? 0.0895 0.1597 0.2272 -0.0072 -0.0157 -0.0347 151 SER A N   
1306 C  CA  A SER A 151 ? 0.0584 0.1911 0.2539 -0.0301 -0.0533 -0.0494 151 SER A CA  
1307 C  CA  B SER A 151 ? 0.1036 0.1875 0.2658 -0.0206 -0.0394 -0.0270 151 SER A CA  
1308 C  C   A SER A 151 ? 0.0831 0.1934 0.2089 -0.0111 -0.0524 -0.0277 151 SER A C   
1309 C  C   B SER A 151 ? 0.0775 0.1824 0.2016 -0.0417 -0.0231 -0.0070 151 SER A C   
1310 O  O   A SER A 151 ? 0.0444 0.1415 0.1687 0.0031  -0.0029 -0.0458 151 SER A O   
1311 O  O   B SER A 151 ? 0.0590 0.1463 0.2234 -0.0491 -0.0409 -0.0250 151 SER A O   
1312 C  CB  A SER A 151 ? 0.0606 0.3224 0.2760 -0.0182 -0.0570 -0.0240 151 SER A CB  
1313 C  CB  B SER A 151 ? 0.1115 0.2108 0.2886 0.0258  -0.0302 0.0289  151 SER A CB  
1314 O  OG  A SER A 151 ? 0.1123 0.4518 0.2619 0.0150  0.0157  0.0103  151 SER A OG  
1315 O  OG  B SER A 151 ? 0.1040 0.2816 0.3226 0.0155  0.0355  -0.0594 151 SER A OG  
1316 N  N   . ALA A 152 ? 0.0757 0.1449 0.2083 -0.0294 -0.0418 -0.0324 152 ALA A N   
1317 C  CA  . ALA A 152 ? 0.1066 0.1331 0.2263 -0.0427 -0.0674 -0.0370 152 ALA A CA  
1318 C  C   . ALA A 152 ? 0.0933 0.1427 0.2142 -0.0568 -0.0717 -0.0585 152 ALA A C   
1319 O  O   . ALA A 152 ? 0.0878 0.1688 0.3019 -0.0659 -0.0312 -0.0017 152 ALA A O   
1320 C  CB  . ALA A 152 ? 0.1489 0.1914 0.2305 -0.0583 -0.1086 -0.0430 152 ALA A CB  
1321 N  N   . LYS A 153 ? 0.1729 0.1235 0.2019 -0.0363 -0.0882 -0.0388 153 LYS A N   
1322 C  CA  . LYS A 153 ? 0.1166 0.1312 0.2444 -0.0420 -0.0453 -0.0442 153 LYS A CA  
1323 C  C   . LYS A 153 ? 0.1326 0.1368 0.2797 -0.0811 -0.0670 -0.0439 153 LYS A C   
1324 O  O   . LYS A 153 ? 0.1469 0.1754 0.2069 -0.0618 -0.1087 -0.0210 153 LYS A O   
1325 C  CB  . LYS A 153 ? 0.1333 0.1262 0.2542 -0.0502 -0.0572 -0.0542 153 LYS A CB  
1326 C  CG  . LYS A 153 ? 0.1990 0.1327 0.2445 -0.0623 -0.0963 -0.0436 153 LYS A CG  
1327 C  CD  . LYS A 153 ? 0.1834 0.1610 0.2619 -0.0952 -0.0798 -0.0231 153 LYS A CD  
1328 C  CE  . LYS A 153 ? 0.2078 0.1863 0.2123 -0.0964 -0.0162 -0.0390 153 LYS A CE  
1329 N  NZ  . LYS A 153 ? 0.0791 0.2579 0.3067 -0.0913 -0.0134 -0.0035 153 LYS A NZ  
1330 N  N   . PRO A 154 ? 0.1399 0.1722 0.2354 -0.0668 -0.0656 -0.0083 154 PRO A N   
1331 C  CA  . PRO A 154 ? 0.1021 0.2245 0.2957 -0.0496 -0.0907 -0.0603 154 PRO A CA  
1332 C  C   . PRO A 154 ? 0.0951 0.2319 0.2439 -0.0444 -0.0590 -0.0336 154 PRO A C   
1333 O  O   . PRO A 154 ? 0.1790 0.2112 0.2478 -0.0244 -0.1183 -0.0797 154 PRO A O   
1334 C  CB  . PRO A 154 ? 0.1059 0.1878 0.3122 -0.0356 -0.0878 -0.0688 154 PRO A CB  
1335 C  CG  . PRO A 154 ? 0.0760 0.3204 0.2812 -0.0884 -0.0381 -0.0959 154 PRO A CG  
1336 C  CD  . PRO A 154 ? 0.1353 0.1956 0.2486 -0.0629 -0.0664 -0.0445 154 PRO A CD  
1337 N  N   . GLY A 155 ? 0.1398 0.1487 0.2812 -0.0842 -0.1138 -0.0501 155 GLY A N   
1338 C  CA  . GLY A 155 ? 0.1815 0.1715 0.3184 -0.0449 -0.1173 -0.0697 155 GLY A CA  
1339 C  C   . GLY A 155 ? 0.2407 0.1167 0.2660 -0.0396 -0.0907 -0.0724 155 GLY A C   
1340 O  O   . GLY A 155 ? 0.2749 0.1330 0.3348 -0.0229 -0.0788 -0.0639 155 GLY A O   
1341 N  N   . LEU A 156 ? 0.1804 0.1247 0.2570 -0.0383 -0.0847 -0.0454 156 LEU A N   
1342 C  CA  . LEU A 156 ? 0.2181 0.1146 0.2312 -0.0332 -0.1002 -0.0434 156 LEU A CA  
1343 C  C   . LEU A 156 ? 0.2790 0.1388 0.2550 0.0027  -0.1038 -0.0483 156 LEU A C   
1344 O  O   . LEU A 156 ? 0.2467 0.1260 0.1971 -0.0315 -0.1182 -0.0529 156 LEU A O   
1345 C  CB  . LEU A 156 ? 0.2118 0.1333 0.2257 -0.0060 -0.1139 -0.0612 156 LEU A CB  
1346 C  CG  . LEU A 156 ? 0.2127 0.1381 0.2090 -0.0095 -0.1158 -0.0691 156 LEU A CG  
1347 C  CD1 . LEU A 156 ? 0.2092 0.1386 0.2473 -0.0084 -0.0911 -0.0849 156 LEU A CD1 
1348 C  CD2 . LEU A 156 ? 0.1739 0.1445 0.1924 -0.0326 -0.0517 -0.0789 156 LEU A CD2 
1349 N  N   . GLN A 157 ? 0.2116 0.1436 0.2092 -0.0130 -0.0886 -0.0697 157 GLN A N   
1350 C  CA  . GLN A 157 ? 0.2526 0.1772 0.2175 -0.0227 -0.1010 -0.0630 157 GLN A CA  
1351 C  C   . GLN A 157 ? 0.2647 0.1772 0.1854 -0.0168 -0.0877 -0.0265 157 GLN A C   
1352 O  O   . GLN A 157 ? 0.2380 0.1515 0.2106 -0.0541 -0.1128 -0.0291 157 GLN A O   
1353 C  CB  . GLN A 157 ? 0.3116 0.1599 0.2021 0.0052  -0.0855 -0.0609 157 GLN A CB  
1354 C  CG  . GLN A 157 ? 0.4687 0.1697 0.1910 -0.0651 -0.0939 -0.0763 157 GLN A CG  
1355 C  CD  . GLN A 157 ? 0.4352 0.1383 0.2241 -0.0357 -0.1613 -0.0401 157 GLN A CD  
1356 O  OE1 . GLN A 157 ? 0.4175 0.1549 0.2239 0.0008  -0.1102 -0.0705 157 GLN A OE1 
1357 N  NE2 . GLN A 157 ? 0.4868 0.1709 0.2379 -0.0211 -0.1569 -0.0049 157 GLN A NE2 
1358 N  N   . LYS A 158 ? 0.2423 0.1807 0.2054 -0.0306 -0.1064 -0.0518 158 LYS A N   
1359 C  CA  . LYS A 158 ? 0.3019 0.1754 0.2181 -0.0250 -0.1141 -0.0603 158 LYS A CA  
1360 C  C   . LYS A 158 ? 0.2785 0.1383 0.1818 -0.0659 -0.0832 -0.0572 158 LYS A C   
1361 O  O   . LYS A 158 ? 0.2892 0.1481 0.2066 -0.0092 -0.0903 -0.0633 158 LYS A O   
1362 C  CB  . LYS A 158 ? 0.2472 0.2218 0.2526 -0.0178 -0.0816 -0.0441 158 LYS A CB  
1363 C  CG  . LYS A 158 ? 0.2753 0.2690 0.5302 -0.0369 -0.1948 -0.0553 158 LYS A CG  
1364 C  CD  . LYS A 158 ? 0.5775 0.3308 0.6299 -0.1562 -0.1965 -0.0053 158 LYS A CD  
1365 C  CE  . LYS A 158 ? 0.5448 0.5887 0.7274 -0.1391 -0.1785 0.0326  158 LYS A CE  
1366 N  NZ  . LYS A 158 ? 0.2933 0.5871 0.3685 -0.0216 -0.0835 -0.1539 158 LYS A NZ  
1367 N  N   . VAL A 159 ? 0.2816 0.1406 0.1855 -0.0468 -0.1092 -0.0316 159 VAL A N   
1368 C  CA  . VAL A 159 ? 0.2846 0.1217 0.1618 -0.0124 -0.0558 -0.0701 159 VAL A CA  
1369 C  C   . VAL A 159 ? 0.2834 0.1275 0.1768 -0.0223 -0.0922 -0.0524 159 VAL A C   
1370 O  O   . VAL A 159 ? 0.2874 0.1441 0.1790 -0.0434 -0.0814 -0.0484 159 VAL A O   
1371 C  CB  . VAL A 159 ? 0.3458 0.1666 0.1836 -0.0399 -0.1291 -0.0394 159 VAL A CB  
1372 C  CG1 . VAL A 159 ? 0.3348 0.2261 0.1667 -0.0452 -0.1181 -0.0665 159 VAL A CG1 
1373 C  CG2 . VAL A 159 ? 0.2930 0.2021 0.2539 -0.0825 -0.1477 -0.0094 159 VAL A CG2 
1374 N  N   . VAL A 160 ? 0.2795 0.1128 0.1967 -0.0306 -0.0823 -0.0490 160 VAL A N   
1375 C  CA  . VAL A 160 ? 0.3283 0.1473 0.2099 -0.0710 -0.0483 -0.0925 160 VAL A CA  
1376 C  C   . VAL A 160 ? 0.2778 0.1801 0.2053 0.0070  -0.0631 -0.0285 160 VAL A C   
1377 O  O   . VAL A 160 ? 0.3511 0.1222 0.2091 -0.0016 -0.0274 -0.0677 160 VAL A O   
1378 C  CB  . VAL A 160 ? 0.4727 0.1399 0.2502 -0.1154 0.0428  -0.0987 160 VAL A CB  
1379 C  CG1 . VAL A 160 ? 0.3862 0.1826 0.3098 -0.0401 -0.0179 -0.0519 160 VAL A CG1 
1380 C  CG2 . VAL A 160 ? 0.4799 0.1770 0.2482 -0.1155 0.0536  -0.0820 160 VAL A CG2 
1381 N  N   . ASP A 161 ? 0.3107 0.1657 0.1768 0.0239  -0.0728 -0.0566 161 ASP A N   
1382 C  CA  . ASP A 161 ? 0.3518 0.1729 0.1782 -0.0006 -0.0831 -0.0359 161 ASP A CA  
1383 C  C   . ASP A 161 ? 0.4361 0.2414 0.1982 0.0740  -0.1307 -0.0572 161 ASP A C   
1384 O  O   . ASP A 161 ? 0.4557 0.2503 0.2190 0.0538  -0.0970 -0.0477 161 ASP A O   
1385 C  CB  . ASP A 161 ? 0.3925 0.2485 0.2093 0.0272  -0.1120 -0.0345 161 ASP A CB  
1386 C  CG  . ASP A 161 ? 0.4172 0.1973 0.2470 -0.0275 -0.0758 -0.1093 161 ASP A CG  
1387 O  OD1 . ASP A 161 ? 0.4446 0.2109 0.3508 -0.0408 -0.1042 -0.1143 161 ASP A OD1 
1388 O  OD2 . ASP A 161 ? 0.4393 0.3383 0.3439 -0.0363 -0.1565 0.0000  161 ASP A OD2 
1389 N  N   . VAL A 162 ? 0.4420 0.1683 0.1833 0.0467  -0.1310 -0.0781 162 VAL A N   
1390 C  CA  . VAL A 162 ? 0.4295 0.1879 0.1899 0.0230  -0.1095 -0.0989 162 VAL A CA  
1391 C  C   . VAL A 162 ? 0.4191 0.1883 0.1540 0.0432  -0.0606 -0.0743 162 VAL A C   
1392 O  O   . VAL A 162 ? 0.4675 0.2004 0.1818 0.0673  -0.0553 -0.0716 162 VAL A O   
1393 C  CB  . VAL A 162 ? 0.4984 0.1735 0.3168 0.0070  -0.1652 -0.0774 162 VAL A CB  
1394 C  CG1 . VAL A 162 ? 0.5340 0.1821 0.2816 -0.0117 -0.0907 -0.0167 162 VAL A CG1 
1395 C  CG2 . VAL A 162 ? 0.6903 0.3689 0.3799 -0.0628 -0.1323 -0.2208 162 VAL A CG2 
1396 N  N   . LEU A 163 ? 0.4826 0.1438 0.1787 0.0232  -0.0347 -0.0549 163 LEU A N   
1397 C  CA  . LEU A 163 ? 0.4854 0.1640 0.1667 0.0212  -0.0177 -0.0528 163 LEU A CA  
1398 C  C   . LEU A 163 ? 0.4447 0.1769 0.1894 0.0339  -0.0181 -0.0475 163 LEU A C   
1399 O  O   . LEU A 163 ? 0.4256 0.1878 0.1766 0.0146  -0.0135 -0.0856 163 LEU A O   
1400 C  CB  . LEU A 163 ? 0.3370 0.1599 0.1636 0.0453  -0.0155 -0.0532 163 LEU A CB  
1401 C  CG  . LEU A 163 ? 0.2825 0.1400 0.1565 0.0042  -0.0307 -0.0780 163 LEU A CG  
1402 C  CD1 . LEU A 163 ? 0.2737 0.1008 0.2020 0.0035  -0.0074 -0.0859 163 LEU A CD1 
1403 C  CD2 . LEU A 163 ? 0.3053 0.1525 0.1818 0.0207  -0.0668 -0.0836 163 LEU A CD2 
1404 N  N   . ASP A 164 ? 0.5407 0.1914 0.1520 0.0747  -0.0038 -0.0458 164 ASP A N   
1405 C  CA  . ASP A 164 ? 0.5355 0.1678 0.1985 0.0922  0.0065  -0.0403 164 ASP A CA  
1406 C  C   . ASP A 164 ? 0.5889 0.2266 0.1806 0.1319  -0.0347 -0.0728 164 ASP A C   
1407 O  O   . ASP A 164 ? 0.6463 0.2550 0.1825 0.0875  0.0189  -0.0732 164 ASP A O   
1408 C  CB  . ASP A 164 ? 0.5012 0.1988 0.2913 0.0334  -0.1012 -0.0218 164 ASP A CB  
1409 C  CG  . ASP A 164 ? 0.4190 0.3717 0.2429 0.1622  -0.1681 -0.0827 164 ASP A CG  
1410 O  OD1 . ASP A 164 ? 0.7534 0.3883 0.3377 0.1578  0.0620  -0.0824 164 ASP A OD1 
1411 O  OD2 . ASP A 164 ? 0.5159 0.6637 0.2639 0.1321  -0.0111 0.0466  164 ASP A OD2 
1412 N  N   . SER A 165 ? 0.5303 0.2283 0.1615 0.1289  -0.0718 -0.0800 165 SER A N   
1413 C  CA  . SER A 165 ? 0.6054 0.2348 0.1697 0.1582  -0.0356 -0.0666 165 SER A CA  
1414 C  C   . SER A 165 ? 0.5188 0.2336 0.1897 0.1139  -0.0520 -0.0980 165 SER A C   
1415 O  O   . SER A 165 ? 0.5872 0.2320 0.1764 0.1390  -0.0641 -0.0739 165 SER A O   
1416 C  CB  . SER A 165 ? 0.6455 0.3270 0.2908 0.1611  -0.0157 -0.0650 165 SER A CB  
1417 O  OG  . SER A 165 ? 0.8071 0.2119 0.2766 0.1092  -0.0529 -0.0762 165 SER A OG  
1418 N  N   . ILE A 166 ? 0.5431 0.1544 0.1421 0.0989  -0.0174 -0.0603 166 ILE A N   
1419 C  CA  . ILE A 166 ? 0.4840 0.2491 0.2396 0.0886  -0.0027 -0.0055 166 ILE A CA  
1420 C  C   . ILE A 166 ? 0.4766 0.1824 0.1820 0.0954  -0.0212 -0.0374 166 ILE A C   
1421 O  O   . ILE A 166 ? 0.5453 0.1909 0.1452 0.1559  0.0147  -0.0496 166 ILE A O   
1422 C  CB  . ILE A 166 ? 0.5200 0.1650 0.1909 0.0892  0.0020  -0.0607 166 ILE A CB  
1423 C  CG1 . ILE A 166 ? 0.4839 0.1861 0.1474 0.0718  -0.0177 -0.0680 166 ILE A CG1 
1424 C  CG2 . ILE A 166 ? 0.5315 0.1676 0.2960 0.1184  -0.0998 -0.0963 166 ILE A CG2 
1425 C  CD1 . ILE A 166 ? 0.3301 0.1800 0.1637 0.0262  -0.0108 -0.0384 166 ILE A CD1 
1426 N  N   . LYS A 167 ? 0.4898 0.2098 0.1866 0.1191  0.0160  -0.0423 167 LYS A N   
1427 C  CA  . LYS A 167 ? 0.4643 0.2105 0.1847 0.1261  0.0241  -0.0380 167 LYS A CA  
1428 C  C   . LYS A 167 ? 0.4481 0.2149 0.1496 0.0884  0.0464  -0.0890 167 LYS A C   
1429 O  O   . LYS A 167 ? 0.4178 0.2195 0.1493 0.1163  0.0239  -0.0511 167 LYS A O   
1430 C  CB  . LYS A 167 ? 0.5720 0.2456 0.1608 0.1384  0.0387  -0.0036 167 LYS A CB  
1431 C  CG  . LYS A 167 ? 0.3177 0.3563 0.2518 0.1424  0.0763  0.0539  167 LYS A CG  
1432 C  CD  . LYS A 167 ? 0.4673 0.3847 0.2749 0.0647  -0.0502 0.0948  167 LYS A CD  
1433 C  CE  . LYS A 167 ? 0.3785 0.5598 0.4072 0.0218  -0.0392 0.1165  167 LYS A CE  
1434 N  NZ  . LYS A 167 ? 0.5313 0.6533 0.5008 0.0917  -0.1252 0.1943  167 LYS A NZ  
1435 N  N   . THR A 168 ? 0.1018 0.1679 0.2393 0.0022  -0.0198 -0.0794 168 THR A N   
1436 C  CA  . THR A 168 ? 0.0403 0.2680 0.2250 -0.0444 -0.0249 -0.0776 168 THR A CA  
1437 C  C   . THR A 168 ? 0.0336 0.1635 0.1236 -0.0628 0.0366  -0.0545 168 THR A C   
1438 O  O   . THR A 168 ? 0.0358 0.2170 0.2638 -0.0756 0.0136  -0.0992 168 THR A O   
1439 C  CB  . THR A 168 ? 0.1981 0.1595 0.3016 -0.0794 -0.0081 -0.0719 168 THR A CB  
1440 O  OG1 . THR A 168 ? 0.1544 0.2229 0.2498 -0.0586 0.0321  -0.0915 168 THR A OG1 
1441 C  CG2 . THR A 168 ? 0.2117 0.2094 0.2268 -0.1177 0.0863  -0.0637 168 THR A CG2 
1442 N  N   . LYS A 169 ? 0.0281 0.2345 0.2427 -0.0055 0.0136  -0.1293 169 LYS A N   
1443 C  CA  . LYS A 169 ? 0.1134 0.1920 0.2353 0.0370  0.0214  -0.1207 169 LYS A CA  
1444 C  C   . LYS A 169 ? 0.0667 0.2222 0.2473 -0.0699 0.0585  -0.1679 169 LYS A C   
1445 O  O   . LYS A 169 ? 0.2771 0.3292 0.2053 0.0955  0.0261  -0.0774 169 LYS A O   
1446 C  CB  . LYS A 169 ? 0.0906 0.1885 0.1929 -0.0342 0.0524  -0.1183 169 LYS A CB  
1447 C  CG  . LYS A 169 ? 0.2522 0.2680 0.2389 0.0839  0.0256  -0.0807 169 LYS A CG  
1448 C  CD  . LYS A 169 ? 0.2051 0.2645 0.3849 -0.0638 0.0763  -0.1978 169 LYS A CD  
1449 C  CE  . LYS A 169 ? 0.0743 0.3376 0.5589 -0.0194 -0.0226 -0.1148 169 LYS A CE  
1450 N  NZ  . LYS A 169 ? 0.5302 0.6104 0.5533 0.1072  0.0872  -0.0479 169 LYS A NZ  
1451 N  N   . GLY A 170 ? 0.0848 0.1804 0.2645 -0.0337 0.0167  -0.1017 170 GLY A N   
1452 C  CA  . GLY A 170 ? 0.1802 0.1887 0.4248 -0.0335 -0.0300 -0.1742 170 GLY A CA  
1453 C  C   . GLY A 170 ? 0.3825 0.1942 0.2566 -0.0842 -0.0792 -0.0664 170 GLY A C   
1454 O  O   . GLY A 170 ? 0.5946 0.1687 0.2325 0.0838  -0.0425 -0.1420 170 GLY A O   
1455 N  N   . LYS A 171 ? 0.0441 0.2714 0.5554 -0.0692 0.0776  -0.2682 171 LYS A N   
1456 C  CA  . LYS A 171 ? 0.0375 0.1678 0.4420 -0.0647 0.0724  -0.0651 171 LYS A CA  
1457 C  C   . LYS A 171 ? 0.1489 0.4663 0.7940 -0.2179 -0.2018 0.0565  171 LYS A C   
1458 O  O   . LYS A 171 ? 0.3208 0.1926 0.3785 0.0783  -0.0704 -0.1503 171 LYS A O   
1459 C  CB  . LYS A 171 ? 0.0596 0.2054 0.3070 -0.0322 -0.0148 -0.0998 171 LYS A CB  
1460 C  CG  . LYS A 171 ? 0.0276 0.1885 0.5623 -0.0460 0.0860  -0.0557 171 LYS A CG  
1461 C  CD  . LYS A 171 ? 0.5167 0.3433 0.4978 0.0910  -0.0149 -0.0739 171 LYS A CD  
1462 C  CE  . LYS A 171 ? 0.5425 0.6545 0.6529 -0.1745 0.1667  0.0910  171 LYS A CE  
1463 N  NZ  . LYS A 171 ? 0.8806 0.7478 0.9710 -0.4780 -0.2816 -0.0548 171 LYS A NZ  
1464 N  N   . SER A 172 ? 0.0381 0.2845 0.3558 -0.0580 -0.0105 -0.2249 172 SER A N   
1465 C  CA  . SER A 172 ? 0.3258 0.5380 1.0398 -0.3339 -0.2212 -0.1696 172 SER A CA  
1466 C  C   . SER A 172 ? 0.0757 0.3085 0.3111 -0.1297 -0.0020 -0.1310 172 SER A C   
1467 O  O   . SER A 172 ? 0.4666 0.2900 0.1941 -0.0378 -0.0401 -0.1301 172 SER A O   
1468 C  CB  . SER A 172 ? 0.0917 0.4110 0.3222 -0.1088 0.0462  -0.1655 172 SER A CB  
1469 O  OG  . SER A 172 ? 0.1559 0.4052 0.3458 -0.0527 -0.0214 -0.1409 172 SER A OG  
1470 N  N   . ALA A 173 ? 0.8728 1.3625 3.1124 -0.9271 -0.4316 -0.5641 173 ALA A N   
1471 C  CA  . ALA A 173 ? 0.5394 1.1052 1.3977 -0.6793 -0.1190 -0.4121 173 ALA A CA  
1472 C  C   . ALA A 173 ? 0.3664 0.7446 0.8523 -0.5149 -0.2797 0.3652  173 ALA A C   
1473 O  O   . ALA A 173 ? 0.2920 0.2240 0.3702 -0.0809 -0.1348 -0.0625 173 ALA A O   
1474 C  CB  . ALA A 173 ? 0.3127 1.2086 1.0332 -0.4549 -0.0105 -0.2921 173 ALA A CB  
1475 N  N   . ASP A 174 ? 0.2389 0.5673 0.3170 -0.2328 -0.0986 -0.1981 174 ASP A N   
1476 C  CA  . ASP A 174 ? 0.2043 0.5405 0.4262 -0.0006 0.1162  0.0315  174 ASP A CA  
1477 C  C   . ASP A 174 ? 0.5040 0.5822 0.4238 -0.0872 0.1583  -0.1194 174 ASP A C   
1478 O  O   . ASP A 174 ? 1.0977 0.8707 0.4574 -0.4170 -0.0245 0.3341  174 ASP A O   
1479 C  CB  . ASP A 174 ? 0.3057 0.6366 0.7765 -0.2642 0.0322  -0.2016 174 ASP A CB  
1480 C  CG  . ASP A 174 ? 0.7244 0.7410 0.8104 -0.1230 0.0682  -0.2155 174 ASP A CG  
1481 O  OD1 . ASP A 174 ? 0.9124 0.7839 0.8963 -0.3852 0.3510  0.0310  174 ASP A OD1 
1482 O  OD2 . ASP A 174 ? 1.1057 0.6732 1.4202 -0.2234 -0.0417 -0.0995 174 ASP A OD2 
1483 N  N   . PHE A 175 ? 0.0732 0.5371 0.3785 0.1196  0.0050  -0.0098 175 PHE A N   
1484 C  CA  . PHE A 175 ? 0.0620 0.3527 0.4875 -0.1388 0.0796  -0.2043 175 PHE A CA  
1485 C  C   . PHE A 175 ? 0.0499 0.2227 1.0378 -0.0824 -0.1362 0.0665  175 PHE A C   
1486 O  O   . PHE A 175 ? 0.5294 0.2220 0.9173 -0.0679 -0.4163 -0.1644 175 PHE A O   
1487 C  CB  . PHE A 175 ? 0.4408 0.1842 0.2610 -0.1423 -0.1585 -0.0972 175 PHE A CB  
1488 C  CG  . PHE A 175 ? 0.4180 0.1639 0.2359 -0.1104 -0.1429 -0.0392 175 PHE A CG  
1489 C  CD1 . PHE A 175 ? 0.4366 0.1504 0.3295 -0.0792 -0.1782 -0.0068 175 PHE A CD1 
1490 C  CD2 . PHE A 175 ? 0.3859 0.1636 0.2196 -0.1039 -0.1183 -0.0175 175 PHE A CD2 
1491 C  CE1 . PHE A 175 ? 0.5231 0.1793 0.2101 -0.0955 -0.1394 -0.0385 175 PHE A CE1 
1492 C  CE2 . PHE A 175 ? 0.4666 0.1463 0.2468 -0.0802 -0.1138 -0.0542 175 PHE A CE2 
1493 C  CZ  . PHE A 175 ? 0.4490 0.1615 0.2247 -0.0763 -0.0596 -0.0457 175 PHE A CZ  
1494 N  N   . THR A 176 ? 0.2144 0.2322 0.2461 -0.0359 -0.1347 -0.1560 176 THR A N   
1495 C  CA  . THR A 176 ? 0.2691 0.2720 0.4186 -0.0556 -0.1035 -0.0622 176 THR A CA  
1496 C  C   . THR A 176 ? 0.2766 0.1587 0.2323 -0.0769 -0.1375 -0.0771 176 THR A C   
1497 O  O   . THR A 176 ? 0.3920 0.1812 0.2311 -0.0100 -0.1360 -0.0895 176 THR A O   
1498 C  CB  . THR A 176 ? 0.5163 0.2440 0.4061 0.0857  -0.0630 -0.0719 176 THR A CB  
1499 O  OG1 . THR A 176 ? 0.5518 0.3040 0.4448 0.0378  -0.0179 0.0120  176 THR A OG1 
1500 C  CG2 . THR A 176 ? 0.5899 0.4255 0.5727 0.2491  -0.0588 -0.0881 176 THR A CG2 
1501 N  N   . ASN A 177 ? 0.3592 0.2429 0.2218 -0.0137 -0.1639 -0.0670 177 ASN A N   
1502 C  CA  . ASN A 177 ? 0.3840 0.1764 0.3055 -0.0154 -0.1709 -0.0751 177 ASN A CA  
1503 C  C   . ASN A 177 ? 0.4322 0.1823 0.2530 -0.0142 -0.1626 -0.0737 177 ASN A C   
1504 O  O   . ASN A 177 ? 0.4249 0.2136 0.3689 0.0098  -0.2184 -0.1558 177 ASN A O   
1505 C  CB  . ASN A 177 ? 0.4341 0.1566 0.3216 -0.0089 -0.2010 -0.1201 177 ASN A CB  
1506 C  CG  . ASN A 177 ? 0.4029 0.1424 0.2669 -0.0632 -0.1287 -0.0904 177 ASN A CG  
1507 O  OD1 . ASN A 177 ? 0.2957 0.2851 0.2922 -0.0809 -0.1017 -0.0438 177 ASN A OD1 
1508 N  ND2 . ASN A 177 ? 0.3075 0.2400 0.2329 -0.0318 -0.1425 -0.1100 177 ASN A ND2 
1509 N  N   . PHE A 178 ? 0.4780 0.1648 0.2592 0.0039  -0.1773 -0.0968 178 PHE A N   
1510 C  CA  . PHE A 178 ? 0.4418 0.1609 0.2557 -0.0009 -0.1295 -0.0973 178 PHE A CA  
1511 C  C   . PHE A 178 ? 0.2113 0.1459 0.2694 -0.0510 -0.1412 -0.0637 178 PHE A C   
1512 O  O   . PHE A 178 ? 0.3865 0.1476 0.2251 -0.0127 -0.1398 -0.0841 178 PHE A O   
1513 C  CB  . PHE A 178 ? 0.4586 0.1412 0.2108 -0.0199 -0.0739 -0.1246 178 PHE A CB  
1514 C  CG  . PHE A 178 ? 0.3907 0.1330 0.2402 -0.0082 -0.1336 -0.1222 178 PHE A CG  
1515 C  CD1 . PHE A 178 ? 0.3416 0.1459 0.2425 -0.0217 -0.1344 -0.0829 178 PHE A CD1 
1516 C  CD2 . PHE A 178 ? 0.2606 0.1299 0.2248 -0.0273 -0.0957 -0.0704 178 PHE A CD2 
1517 C  CE1 . PHE A 178 ? 0.3864 0.1592 0.2371 0.0208  -0.1389 -0.0934 178 PHE A CE1 
1518 C  CE2 . PHE A 178 ? 0.2078 0.1421 0.1812 -0.0357 -0.0971 -0.0639 178 PHE A CE2 
1519 C  CZ  . PHE A 178 ? 0.2724 0.1245 0.2119 -0.0566 -0.1034 -0.0696 178 PHE A CZ  
1520 N  N   . ASP A 179 ? 0.2507 0.1800 0.2272 -0.0254 -0.1509 -0.0648 179 ASP A N   
1521 C  CA  . ASP A 179 ? 0.1870 0.1923 0.2499 -0.0398 -0.1277 -0.0883 179 ASP A CA  
1522 C  C   . ASP A 179 ? 0.2320 0.1125 0.2592 -0.0602 -0.1302 -0.0589 179 ASP A C   
1523 O  O   . ASP A 179 ? 0.2123 0.1335 0.2502 -0.0542 -0.1390 -0.0497 179 ASP A O   
1524 C  CB  . ASP A 179 ? 0.1947 0.2492 0.2943 -0.0181 -0.1294 -0.0835 179 ASP A CB  
1525 C  CG  . ASP A 179 ? 0.2158 0.2740 0.3180 -0.0074 -0.1275 -0.0824 179 ASP A CG  
1526 O  OD1 . ASP A 179 ? 0.1733 0.1764 0.3351 -0.0339 -0.1323 -0.0890 179 ASP A OD1 
1527 O  OD2 . ASP A 179 ? 0.2084 0.4132 0.4354 -0.0389 -0.1307 -0.0832 179 ASP A OD2 
1528 N  N   . PRO A 180 ? 0.1662 0.1280 0.2279 -0.0583 -0.1065 -0.0571 180 PRO A N   
1529 C  CA  . PRO A 180 ? 0.1610 0.1719 0.2013 -0.0556 -0.0974 -0.0678 180 PRO A CA  
1530 C  C   . PRO A 180 ? 0.1106 0.1722 0.1922 -0.0479 -0.1037 -0.0479 180 PRO A C   
1531 O  O   . PRO A 180 ? 0.0998 0.1637 0.1761 -0.0719 -0.0512 -0.0475 180 PRO A O   
1532 C  CB  . PRO A 180 ? 0.1613 0.1620 0.2260 -0.0468 -0.0963 -0.0683 180 PRO A CB  
1533 C  CG  . PRO A 180 ? 0.1710 0.1617 0.2469 -0.0614 -0.1225 -0.0468 180 PRO A CG  
1534 C  CD  . PRO A 180 ? 0.1416 0.1597 0.2368 -0.0640 -0.0996 -0.0417 180 PRO A CD  
1535 N  N   . ARG A 181 ? 0.1007 0.1690 0.2365 -0.0280 -0.1032 -0.0432 181 ARG A N   
1536 C  CA  . ARG A 181 ? 0.0893 0.1692 0.2570 -0.0629 -0.0751 -0.0260 181 ARG A CA  
1537 C  C   . ARG A 181 ? 0.0868 0.1846 0.2669 -0.0641 -0.0754 -0.0254 181 ARG A C   
1538 O  O   . ARG A 181 ? 0.0903 0.2007 0.3023 -0.0771 -0.0549 -0.0573 181 ARG A O   
1539 C  CB  . ARG A 181 ? 0.0760 0.1729 0.2896 -0.0557 -0.0700 -0.0346 181 ARG A CB  
1540 C  CG  . ARG A 181 ? 0.1364 0.1974 0.3589 -0.0869 -0.0950 -0.0136 181 ARG A CG  
1541 C  CD  . ARG A 181 ? 0.1900 0.1808 0.3683 -0.1032 0.0368  -0.0495 181 ARG A CD  
1542 N  NE  . ARG A 181 ? 0.2263 0.2260 0.4333 -0.1042 -0.0332 -0.0949 181 ARG A NE  
1543 C  CZ  . ARG A 181 ? 0.2005 0.3656 0.5072 -0.1172 -0.0537 -0.1186 181 ARG A CZ  
1544 N  NH1 . ARG A 181 ? 0.2940 0.3001 0.5279 -0.0978 -0.0722 -0.1430 181 ARG A NH1 
1545 N  NH2 . ARG A 181 ? 0.3673 0.3983 0.5094 -0.1578 -0.0482 -0.0917 181 ARG A NH2 
1546 N  N   . GLY A 182 ? 0.1921 0.1435 0.2432 -0.1086 -0.1057 -0.0521 182 GLY A N   
1547 C  CA  . GLY A 182 ? 0.2037 0.1518 0.2493 -0.0732 -0.1497 -0.0472 182 GLY A CA  
1548 C  C   . GLY A 182 ? 0.1197 0.1493 0.2441 -0.0681 -0.0749 -0.0540 182 GLY A C   
1549 O  O   . GLY A 182 ? 0.2559 0.1552 0.2653 -0.0771 -0.1245 -0.0402 182 GLY A O   
1550 N  N   . LEU A 183 ? 0.1729 0.1276 0.2505 -0.0545 -0.1226 -0.0567 183 LEU A N   
1551 C  CA  . LEU A 183 ? 0.1581 0.1339 0.2079 -0.0775 -0.0872 -0.0300 183 LEU A CA  
1552 C  C   . LEU A 183 ? 0.1124 0.1048 0.2268 -0.0631 -0.0931 -0.0362 183 LEU A C   
1553 O  O   . LEU A 183 ? 0.0957 0.1436 0.2477 -0.0741 -0.0752 -0.0535 183 LEU A O   
1554 C  CB  . LEU A 183 ? 0.1587 0.1839 0.2460 -0.0715 -0.1260 -0.0802 183 LEU A CB  
1555 C  CG  . LEU A 183 ? 0.2348 0.1597 0.2098 -0.0954 -0.1280 -0.0688 183 LEU A CG  
1556 C  CD1 . LEU A 183 ? 0.3137 0.1727 0.2369 -0.0586 -0.1113 -0.1051 183 LEU A CD1 
1557 C  CD2 . LEU A 183 ? 0.3529 0.1794 0.2485 -0.0926 -0.0867 -0.0569 183 LEU A CD2 
1558 N  N   . LEU A 184 ? 0.1228 0.1746 0.2313 -0.0702 -0.0963 -0.0438 184 LEU A N   
1559 C  CA  . LEU A 184 ? 0.1134 0.1339 0.2264 -0.0380 -0.0996 -0.0617 184 LEU A CA  
1560 C  C   . LEU A 184 ? 0.0858 0.1751 0.3343 -0.0388 -0.0683 -0.0979 184 LEU A C   
1561 O  O   . LEU A 184 ? 0.3574 0.4084 0.5317 0.1037  -0.2676 -0.0134 184 LEU A O   
1562 C  CB  . LEU A 184 ? 0.0500 0.1502 0.2547 -0.0250 -0.0761 -0.0584 184 LEU A CB  
1563 C  CG  . LEU A 184 ? 0.0409 0.1493 0.2561 -0.0503 -0.0371 -0.0664 184 LEU A CG  
1564 C  CD1 . LEU A 184 ? 0.0717 0.1373 0.2223 -0.0438 -0.0238 -0.0517 184 LEU A CD1 
1565 C  CD2 . LEU A 184 ? 0.0491 0.1873 0.2502 -0.0679 -0.0450 -0.0471 184 LEU A CD2 
1566 N  N   . PRO A 185 ? 0.0638 0.1711 0.2831 -0.0292 -0.0920 -0.0727 185 PRO A N   
1567 C  CA  . PRO A 185 ? 0.0560 0.1642 0.3335 -0.0428 -0.0876 -0.0690 185 PRO A CA  
1568 C  C   . PRO A 185 ? 0.0315 0.1674 0.3163 -0.0020 -0.0796 -0.0699 185 PRO A C   
1569 O  O   . PRO A 185 ? 0.1743 0.1591 0.5901 0.0199  -0.0347 -0.0835 185 PRO A O   
1570 C  CB  . PRO A 185 ? 0.0342 0.1937 0.2984 -0.0469 -0.0389 -0.0944 185 PRO A CB  
1571 C  CG  . PRO A 185 ? 0.0604 0.1942 0.2186 -0.0892 -0.0198 -0.0584 185 PRO A CG  
1572 C  CD  . PRO A 185 ? 0.0416 0.1436 0.1724 -0.0343 -0.0321 -0.0335 185 PRO A CD  
1573 N  N   . GLU A 186 ? 0.0326 0.1426 0.3294 -0.0313 -0.0520 -0.0589 186 GLU A N   
1574 C  CA  . GLU A 186 ? 0.0360 0.1956 0.4824 -0.0300 -0.0537 -0.0316 186 GLU A CA  
1575 C  C   . GLU A 186 ? 0.0428 0.1483 0.4116 -0.0545 -0.0002 -0.0763 186 GLU A C   
1576 O  O   . GLU A 186 ? 0.0295 0.1791 0.5666 -0.0590 -0.0184 -0.0639 186 GLU A O   
1577 C  CB  . GLU A 186 ? 0.0960 0.2256 0.5344 0.0307  -0.0397 -0.0257 186 GLU A CB  
1578 C  CG  . GLU A 186 ? 0.2525 0.2087 0.5815 0.0039  -0.0701 0.0152  186 GLU A CG  
1579 C  CD  . GLU A 186 ? 0.2684 0.1897 0.5506 -0.0841 0.1072  0.0551  186 GLU A CD  
1580 O  OE1 . GLU A 186 ? 0.3064 0.2509 0.8034 -0.1090 -0.1264 0.0509  186 GLU A OE1 
1581 O  OE2 . GLU A 186 ? 0.0619 0.2927 0.6010 0.0433  0.0628  -0.0579 186 GLU A OE2 
1582 N  N   . SER A 187 ? 0.0136 0.1982 0.4576 -0.0276 -0.0308 -0.0487 187 SER A N   
1583 C  CA  . SER A 187 ? 0.0190 0.1627 0.4368 -0.0366 0.0600  -0.0879 187 SER A CA  
1584 C  C   . SER A 187 ? 0.0146 0.1503 0.3407 -0.0342 0.0204  -0.0557 187 SER A C   
1585 O  O   . SER A 187 ? 0.0170 0.2112 0.3323 -0.0435 0.0254  -0.0179 187 SER A O   
1586 C  CB  . SER A 187 ? 0.0780 0.1614 0.3709 -0.0365 0.0200  -0.0649 187 SER A CB  
1587 O  OG  . SER A 187 ? 0.0414 0.1911 0.4361 -0.0238 0.0527  -0.0257 187 SER A OG  
1588 N  N   . LEU A 188 ? 0.0152 0.1782 0.4065 -0.0239 0.0280  0.0049  188 LEU A N   
1589 C  CA  . LEU A 188 ? 0.0168 0.1523 0.3305 -0.0257 0.0104  -0.0194 188 LEU A CA  
1590 C  C   . LEU A 188 ? 0.0227 0.1913 0.2841 -0.0182 0.0239  -0.0234 188 LEU A C   
1591 O  O   . LEU A 188 ? 0.0142 0.2348 0.3251 -0.0133 0.0287  0.0116  188 LEU A O   
1592 C  CB  . LEU A 188 ? 0.0502 0.1505 0.4211 -0.0096 0.0409  -0.0514 188 LEU A CB  
1593 C  CG  . LEU A 188 ? 0.0444 0.3421 0.5676 -0.0097 -0.0179 -0.1023 188 LEU A CG  
1594 C  CD1 . LEU A 188 ? 0.2896 0.1764 0.4875 -0.0001 -0.0432 -0.0132 188 LEU A CD1 
1595 C  CD2 . LEU A 188 ? 0.2245 0.2752 0.4367 0.0231  0.0179  -0.0536 188 LEU A CD2 
1596 N  N   . ASP A 189 ? 0.0298 0.2047 0.2996 -0.0644 0.0380  -0.0335 189 ASP A N   
1597 C  CA  . ASP A 189 ? 0.0122 0.2152 0.2619 -0.0104 0.0277  -0.0183 189 ASP A CA  
1598 C  C   . ASP A 189 ? 0.0207 0.1557 0.1752 -0.0387 0.0302  -0.0214 189 ASP A C   
1599 O  O   . ASP A 189 ? 0.0128 0.1586 0.1918 -0.0184 0.0314  -0.0312 189 ASP A O   
1600 C  CB  . ASP A 189 ? 0.0272 0.2558 0.2619 0.0067  0.0166  -0.0662 189 ASP A CB  
1601 C  CG  . ASP A 189 ? 0.1168 0.6047 0.2476 0.0684  0.0789  -0.0498 189 ASP A CG  
1602 O  OD1 . ASP A 189 ? 0.3790 0.6037 0.5909 0.0013  -0.0151 0.0792  189 ASP A OD1 
1603 O  OD2 . ASP A 189 ? 0.3501 0.6574 0.3604 -0.0111 -0.0738 -0.0712 189 ASP A OD2 
1604 N  N   . TYR A 190 ? 0.0174 0.1668 0.1784 -0.0257 0.0395  -0.0360 190 TYR A N   
1605 C  CA  . TYR A 190 ? 0.0155 0.1447 0.1511 -0.0188 0.0345  -0.0313 190 TYR A CA  
1606 C  C   . TYR A 190 ? 0.0172 0.1358 0.1443 -0.0263 0.0339  -0.0365 190 TYR A C   
1607 O  O   . TYR A 190 ? 0.0259 0.1560 0.1637 -0.0337 0.0486  -0.0258 190 TYR A O   
1608 C  CB  . TYR A 190 ? 0.0290 0.1420 0.1969 -0.0433 0.0502  -0.0354 190 TYR A CB  
1609 C  CG  . TYR A 190 ? 0.0201 0.1429 0.1801 -0.0430 0.0188  -0.0374 190 TYR A CG  
1610 C  CD1 . TYR A 190 ? 0.0152 0.1687 0.1672 -0.0076 0.0376  -0.0450 190 TYR A CD1 
1611 C  CD2 . TYR A 190 ? 0.0248 0.1292 0.2021 -0.0423 0.0403  -0.0387 190 TYR A CD2 
1612 C  CE1 . TYR A 190 ? 0.0158 0.1554 0.1776 -0.0111 0.0122  -0.0368 190 TYR A CE1 
1613 C  CE2 . TYR A 190 ? 0.0669 0.1405 0.1799 -0.0171 0.0166  -0.0302 190 TYR A CE2 
1614 C  CZ  . TYR A 190 ? 0.0256 0.1424 0.1827 -0.0219 0.0261  -0.0367 190 TYR A CZ  
1615 O  OH  . TYR A 190 ? 0.0754 0.1978 0.2005 -0.0176 0.0357  0.0044  190 TYR A OH  
1616 N  N   . TRP A 191 ? 0.0162 0.1225 0.1340 -0.0338 0.0182  -0.0592 191 TRP A N   
1617 C  CA  . TRP A 191 ? 0.0191 0.1171 0.1336 -0.0358 0.0286  -0.0555 191 TRP A CA  
1618 C  C   . TRP A 191 ? 0.0137 0.1312 0.1115 -0.0292 0.0190  -0.0527 191 TRP A C   
1619 O  O   . TRP A 191 ? 0.0136 0.1429 0.1277 -0.0131 0.0223  -0.0351 191 TRP A O   
1620 C  CB  . TRP A 191 ? 0.0340 0.1235 0.1445 -0.0567 0.0213  -0.0339 191 TRP A CB  
1621 C  CG  . TRP A 191 ? 0.0270 0.1458 0.1752 -0.0528 0.0341  -0.0656 191 TRP A CG  
1622 C  CD1 . TRP A 191 ? 0.0780 0.1337 0.1798 -0.0398 0.0313  -0.0516 191 TRP A CD1 
1623 C  CD2 . TRP A 191 ? 0.0236 0.1550 0.1762 -0.0505 0.0187  -0.0634 191 TRP A CD2 
1624 N  NE1 . TRP A 191 ? 0.0554 0.1414 0.2106 -0.0337 0.0254  -0.0649 191 TRP A NE1 
1625 C  CE2 . TRP A 191 ? 0.0403 0.1300 0.2108 -0.0641 0.0366  -0.0488 191 TRP A CE2 
1626 C  CE3 . TRP A 191 ? 0.0221 0.2059 0.1787 -0.0553 0.0038  -0.0447 191 TRP A CE3 
1627 C  CZ2 . TRP A 191 ? 0.0383 0.1333 0.2189 -0.0257 -0.0122 -0.0684 191 TRP A CZ2 
1628 C  CZ3 . TRP A 191 ? 0.0212 0.2265 0.2172 -0.0562 0.0210  -0.0418 191 TRP A CZ3 
1629 C  CH2 . TRP A 191 ? 0.0318 0.1895 0.2188 -0.0665 0.0253  -0.0250 191 TRP A CH2 
1630 N  N   . THR A 192 ? 0.0317 0.0991 0.1124 -0.0485 0.0280  -0.0533 192 THR A N   
1631 C  CA  . THR A 192 ? 0.0289 0.1062 0.1242 -0.0471 0.0190  -0.0523 192 THR A CA  
1632 C  C   . THR A 192 ? 0.0304 0.1195 0.1088 -0.0513 0.0274  -0.0425 192 THR A C   
1633 O  O   . THR A 192 ? 0.0172 0.1421 0.1333 -0.0344 0.0280  -0.0507 192 THR A O   
1634 C  CB  . THR A 192 ? 0.0289 0.1125 0.1361 -0.0488 0.0243  -0.0440 192 THR A CB  
1635 O  OG1 . THR A 192 ? 0.0251 0.1075 0.1506 -0.0435 0.0188  -0.0424 192 THR A OG1 
1636 C  CG2 . THR A 192 ? 0.0908 0.1019 0.1340 -0.0549 0.0513  -0.0478 192 THR A CG2 
1637 N  N   . TYR A 193 ? 0.0223 0.1236 0.1105 -0.0411 0.0038  -0.0434 193 TYR A N   
1638 C  CA  . TYR A 193 ? 0.0329 0.1295 0.1285 -0.0507 -0.0010 -0.0543 193 TYR A CA  
1639 C  C   . TYR A 193 ? 0.0249 0.1253 0.1170 -0.0469 0.0091  -0.0254 193 TYR A C   
1640 O  O   . TYR A 193 ? 0.0256 0.1421 0.1180 -0.0510 0.0157  -0.0358 193 TYR A O   
1641 C  CB  . TYR A 193 ? 0.0353 0.1155 0.1176 -0.0520 0.0018  -0.0454 193 TYR A CB  
1642 C  CG  . TYR A 193 ? 0.0293 0.1173 0.1264 -0.0486 0.0093  -0.0501 193 TYR A CG  
1643 C  CD1 . TYR A 193 ? 0.0363 0.1019 0.1118 -0.0518 0.0099  -0.0425 193 TYR A CD1 
1644 C  CD2 . TYR A 193 ? 0.0245 0.1119 0.1107 -0.0423 0.0070  -0.0440 193 TYR A CD2 
1645 C  CE1 . TYR A 193 ? 0.0284 0.1236 0.1201 -0.0489 0.0185  -0.0700 193 TYR A CE1 
1646 C  CE2 . TYR A 193 ? 0.0273 0.1095 0.1105 -0.0466 0.0164  -0.0354 193 TYR A CE2 
1647 C  CZ  . TYR A 193 ? 0.0223 0.0967 0.1054 -0.0355 0.0026  -0.0389 193 TYR A CZ  
1648 O  OH  . TYR A 193 ? 0.0247 0.1001 0.1117 -0.0387 0.0017  -0.0391 193 TYR A OH  
1649 N  N   . PRO A 194 ? 0.0307 0.1198 0.1228 -0.0494 0.0002  -0.0397 194 PRO A N   
1650 C  CA  . PRO A 194 ? 0.0316 0.1367 0.1431 -0.0568 0.0103  -0.0417 194 PRO A CA  
1651 C  C   . PRO A 194 ? 0.0284 0.1235 0.1247 -0.0493 0.0001  -0.0287 194 PRO A C   
1652 O  O   . PRO A 194 ? 0.0370 0.1386 0.1433 -0.0592 -0.0020 -0.0458 194 PRO A O   
1653 C  CB  . PRO A 194 ? 0.0436 0.1280 0.1568 -0.0655 0.0113  -0.0501 194 PRO A CB  
1654 C  CG  . PRO A 194 ? 0.0563 0.1420 0.1430 -0.0340 0.0037  -0.0424 194 PRO A CG  
1655 C  CD  . PRO A 194 ? 0.0177 0.1588 0.1356 -0.0344 0.0270  -0.0335 194 PRO A CD  
1656 N  N   . GLY A 195 ? 0.0299 0.1100 0.1196 -0.0492 0.0102  -0.0309 195 GLY A N   
1657 C  CA  . GLY A 195 ? 0.0454 0.1418 0.1324 -0.0720 0.0157  -0.0466 195 GLY A CA  
1658 C  C   . GLY A 195 ? 0.0141 0.1317 0.1324 -0.0262 -0.0103 -0.0296 195 GLY A C   
1659 O  O   . GLY A 195 ? 0.0152 0.1267 0.1333 -0.0322 0.0062  -0.0422 195 GLY A O   
1660 N  N   . SER A 196 ? 0.0205 0.1005 0.1202 -0.0330 0.0008  -0.0456 196 SER A N   
1661 C  CA  . SER A 196 ? 0.0289 0.0984 0.1502 -0.0455 0.0244  -0.0521 196 SER A CA  
1662 C  C   . SER A 196 ? 0.0350 0.0816 0.1532 -0.0456 0.0187  -0.0490 196 SER A C   
1663 O  O   . SER A 196 ? 0.0204 0.1022 0.1259 -0.0367 0.0179  -0.0447 196 SER A O   
1664 C  CB  . SER A 196 ? 0.0171 0.1101 0.1543 -0.0322 -0.0039 -0.0208 196 SER A CB  
1665 O  OG  . SER A 196 ? 0.0130 0.1066 0.1727 -0.0257 0.0049  -0.0331 196 SER A OG  
1666 N  N   . LEU A 197 ? 0.0222 0.1213 0.1527 -0.0395 -0.0023 -0.0442 197 LEU A N   
1667 C  CA  . LEU A 197 ? 0.0158 0.0972 0.1549 -0.0292 0.0105  -0.0416 197 LEU A CA  
1668 C  C   . LEU A 197 ? 0.0182 0.1098 0.1449 -0.0341 0.0124  -0.0607 197 LEU A C   
1669 O  O   . LEU A 197 ? 0.0183 0.1366 0.1209 -0.0389 0.0004  -0.0220 197 LEU A O   
1670 C  CB  . LEU A 197 ? 0.0202 0.1265 0.1662 -0.0398 0.0112  -0.0615 197 LEU A CB  
1671 C  CG  . LEU A 197 ? 0.0339 0.1159 0.1466 -0.0318 0.0065  -0.0463 197 LEU A CG  
1672 C  CD1 . LEU A 197 ? 0.0429 0.1243 0.1893 -0.0387 0.0292  -0.0638 197 LEU A CD1 
1673 C  CD2 . LEU A 197 ? 0.0571 0.1816 0.2092 -0.0938 0.0381  -0.0875 197 LEU A CD2 
1674 N  N   . THR A 198 ? 0.0261 0.1157 0.1337 -0.0463 0.0170  -0.0304 198 THR A N   
1675 C  CA  . THR A 198 ? 0.0160 0.0968 0.1681 -0.0295 0.0082  -0.0237 198 THR A CA  
1676 C  C   . THR A 198 ? 0.0132 0.0884 0.1588 -0.0226 0.0143  -0.0173 198 THR A C   
1677 O  O   . THR A 198 ? 0.0165 0.0985 0.1794 -0.0299 0.0206  -0.0339 198 THR A O   
1678 C  CB  . THR A 198 ? 0.0144 0.1044 0.1411 -0.0268 0.0144  -0.0169 198 THR A CB  
1679 O  OG1 . THR A 198 ? 0.0162 0.0944 0.1251 -0.0291 0.0175  -0.0397 198 THR A OG1 
1680 C  CG2 . THR A 198 ? 0.0314 0.1064 0.1466 -0.0499 0.0185  -0.0469 198 THR A CG2 
1681 N  N   . THR A 199 ? 0.0293 0.1188 0.1633 -0.0497 0.0288  -0.0383 199 THR A N   
1682 C  CA  . THR A 199 ? 0.0142 0.1317 0.1594 -0.0146 0.0328  -0.0219 199 THR A CA  
1683 C  C   . THR A 199 ? 0.0112 0.1357 0.1634 -0.0141 0.0245  -0.0175 199 THR A C   
1684 O  O   . THR A 199 ? 0.0156 0.1297 0.1670 -0.0097 0.0385  -0.0362 199 THR A O   
1685 C  CB  . THR A 199 ? 0.0353 0.1773 0.2001 -0.0226 -0.0182 -0.0016 199 THR A CB  
1686 O  OG1 . THR A 199 ? 0.0656 0.1939 0.2840 -0.0550 -0.0230 -0.0342 199 THR A OG1 
1687 C  CG2 . THR A 199 ? 0.0381 0.1452 0.1826 -0.0010 0.0031  -0.0245 199 THR A CG2 
1688 N  N   . PRO A 200 ? 0.0132 0.1355 0.1947 -0.0214 0.0261  -0.0073 200 PRO A N   
1689 C  CA  . PRO A 200 ? 0.0316 0.1353 0.2126 -0.0267 0.0694  -0.0346 200 PRO A CA  
1690 C  C   . PRO A 200 ? 0.0155 0.1168 0.2058 -0.0170 0.0402  -0.0320 200 PRO A C   
1691 O  O   . PRO A 200 ? 0.0479 0.1829 0.1946 -0.0210 0.0411  -0.0329 200 PRO A O   
1692 C  CB  . PRO A 200 ? 0.0351 0.2232 0.3065 -0.0402 0.0860  -0.0370 200 PRO A CB  
1693 C  CG  . PRO A 200 ? 0.0244 0.2006 0.2230 -0.0166 0.0553  0.0305  200 PRO A CG  
1694 C  CD  . PRO A 200 ? 0.0251 0.2209 0.2257 -0.0430 0.0424  0.0222  200 PRO A CD  
1695 N  N   . PRO A 201 ? 0.0310 0.1550 0.1621 -0.0088 0.0494  -0.0298 201 PRO A N   
1696 C  CA  . PRO A 201 ? 0.0757 0.1437 0.1712 0.0003  0.0423  -0.0242 201 PRO A CA  
1697 C  C   . PRO A 201 ? 0.0192 0.1430 0.1737 -0.0129 0.0359  -0.0245 201 PRO A C   
1698 O  O   . PRO A 201 ? 0.0183 0.1281 0.1974 -0.0216 0.0259  -0.0205 201 PRO A O   
1699 C  CB  . PRO A 201 ? 0.0407 0.1520 0.2463 -0.0438 0.0622  -0.0403 201 PRO A CB  
1700 C  CG  . PRO A 201 ? 0.0682 0.1393 0.2441 -0.0530 0.0502  -0.0449 201 PRO A CG  
1701 C  CD  . PRO A 201 ? 0.1037 0.1257 0.2289 -0.0279 0.0511  -0.0308 201 PRO A CD  
1702 N  N   . LEU A 202 ? 0.0159 0.1262 0.1814 -0.0329 0.0209  -0.0444 202 LEU A N   
1703 C  CA  . LEU A 202 ? 0.0189 0.1103 0.1591 -0.0358 0.0132  -0.0235 202 LEU A CA  
1704 C  C   . LEU A 202 ? 0.0133 0.1208 0.1865 -0.0214 0.0278  -0.0256 202 LEU A C   
1705 O  O   . LEU A 202 ? 0.0212 0.1314 0.2057 -0.0424 0.0205  -0.0324 202 LEU A O   
1706 C  CB  . LEU A 202 ? 0.0315 0.0955 0.1852 -0.0365 -0.0130 -0.0173 202 LEU A CB  
1707 C  CG  . LEU A 202 ? 0.0189 0.1230 0.2085 -0.0380 0.0093  -0.0127 202 LEU A CG  
1708 C  CD1 . LEU A 202 ? 0.0185 0.1951 0.2627 -0.0443 0.0197  0.0058  202 LEU A CD1 
1709 C  CD2 . LEU A 202 ? 0.0205 0.1124 0.2049 -0.0363 -0.0097 -0.0245 202 LEU A CD2 
1710 N  N   . ALA A 203 ? 0.0106 0.1087 0.1899 -0.0201 0.0117  -0.0270 203 ALA A N   
1711 C  CA  . ALA A 203 ? 0.0344 0.1003 0.1608 -0.0178 0.0181  -0.0380 203 ALA A CA  
1712 C  C   . ALA A 203 ? 0.0181 0.1028 0.1758 -0.0335 0.0152  -0.0328 203 ALA A C   
1713 O  O   . ALA A 203 ? 0.0160 0.1101 0.1559 -0.0297 -0.0039 -0.0302 203 ALA A O   
1714 C  CB  . ALA A 203 ? 0.0201 0.1046 0.2014 -0.0367 0.0222  -0.0465 203 ALA A CB  
1715 N  N   . GLU A 204 ? 0.0179 0.1258 0.1748 -0.0371 0.0040  -0.0200 204 GLU A N   
1716 C  CA  . GLU A 204 ? 0.0207 0.1356 0.1398 -0.0368 -0.0070 -0.0490 204 GLU A CA  
1717 C  C   . GLU A 204 ? 0.0300 0.1195 0.1535 -0.0423 -0.0258 -0.0201 204 GLU A C   
1718 O  O   . GLU A 204 ? 0.0319 0.1588 0.1717 -0.0575 -0.0191 -0.0155 204 GLU A O   
1719 C  CB  . GLU A 204 ? 0.0407 0.1382 0.1838 -0.0575 -0.0358 -0.0102 204 GLU A CB  
1720 C  CG  . GLU A 204 ? 0.0575 0.1626 0.2261 -0.0781 -0.0350 -0.0317 204 GLU A CG  
1721 C  CD  . GLU A 204 ? 0.0405 0.1604 0.2166 -0.0579 -0.0439 -0.0182 204 GLU A CD  
1722 O  OE1 . GLU A 204 ? 0.0514 0.2002 0.2646 -0.0758 -0.0650 0.0053  204 GLU A OE1 
1723 O  OE2 . GLU A 204 ? 0.0284 0.1396 0.2139 -0.0395 -0.0396 -0.0220 204 GLU A OE2 
1724 N  N   . CYS A 205 ? 0.0205 0.1057 0.1623 -0.0340 -0.0074 -0.0351 205 CYS A N   
1725 C  CA  . CYS A 205 ? 0.0142 0.1088 0.1827 -0.0277 0.0068  -0.0555 205 CYS A CA  
1726 C  C   . CYS A 205 ? 0.0148 0.1167 0.1697 -0.0273 -0.0047 -0.0438 205 CYS A C   
1727 O  O   . CYS A 205 ? 0.0218 0.1134 0.1875 -0.0351 -0.0096 -0.0482 205 CYS A O   
1728 C  CB  . CYS A 205 ? 0.0129 0.1395 0.1734 -0.0293 0.0063  -0.0458 205 CYS A CB  
1729 S  SG  . CYS A 205 ? 0.0392 0.1156 0.1535 -0.0453 0.0026  -0.0406 205 CYS A SG  
1730 N  N   . VAL A 206 ? 0.0115 0.1105 0.1418 -0.0200 -0.0061 -0.0342 206 VAL A N   
1731 C  CA  . VAL A 206 ? 0.0092 0.1088 0.1306 -0.0171 0.0033  -0.0332 206 VAL A CA  
1732 C  C   . VAL A 206 ? 0.0205 0.0809 0.1244 -0.0305 0.0052  -0.0430 206 VAL A C   
1733 O  O   . VAL A 206 ? 0.0224 0.1163 0.1387 -0.0410 0.0145  -0.0611 206 VAL A O   
1734 C  CB  . VAL A 206 ? 0.0151 0.1027 0.1385 -0.0269 0.0005  -0.0438 206 VAL A CB  
1735 C  CG1 . VAL A 206 ? 0.0249 0.1173 0.1864 -0.0328 -0.0272 -0.0375 206 VAL A CG1 
1736 C  CG2 . VAL A 206 ? 0.0316 0.1097 0.1348 -0.0488 0.0090  -0.0507 206 VAL A CG2 
1737 N  N   . THR A 207 ? 0.0239 0.0810 0.1373 -0.0338 0.0042  -0.0430 207 THR A N   
1738 C  CA  . THR A 207 ? 0.0233 0.1068 0.1228 -0.0411 0.0170  -0.0493 207 THR A CA  
1739 C  C   . THR A 207 ? 0.0166 0.0981 0.1104 -0.0306 0.0220  -0.0592 207 THR A C   
1740 O  O   . THR A 207 ? 0.0231 0.0988 0.1115 -0.0390 0.0124  -0.0403 207 THR A O   
1741 C  CB  . THR A 207 ? 0.0288 0.1277 0.1560 -0.0520 0.0202  -0.0566 207 THR A CB  
1742 O  OG1 . THR A 207 ? 0.0238 0.1393 0.1769 -0.0471 0.0234  -0.0324 207 THR A OG1 
1743 C  CG2 . THR A 207 ? 0.0227 0.1432 0.1816 -0.0436 0.0380  -0.0584 207 THR A CG2 
1744 N  N   . TRP A 208 ? 0.0218 0.1052 0.1226 -0.0388 0.0182  -0.0577 208 TRP A N   
1745 C  CA  . TRP A 208 ? 0.0211 0.0956 0.1526 -0.0348 0.0153  -0.0666 208 TRP A CA  
1746 C  C   . TRP A 208 ? 0.0146 0.1053 0.1192 -0.0284 0.0078  -0.0373 208 TRP A C   
1747 O  O   . TRP A 208 ? 0.0241 0.1312 0.1324 -0.0459 0.0059  -0.0420 208 TRP A O   
1748 C  CB  . TRP A 208 ? 0.0282 0.1058 0.1190 -0.0433 0.0110  -0.0596 208 TRP A CB  
1749 C  CG  . TRP A 208 ? 0.0271 0.0915 0.1281 -0.0409 0.0108  -0.0439 208 TRP A CG  
1750 C  CD1 . TRP A 208 ? 0.0181 0.1183 0.0930 -0.0278 -0.0064 -0.0272 208 TRP A CD1 
1751 C  CD2 . TRP A 208 ? 0.0264 0.0951 0.1283 -0.0423 0.0163  -0.0335 208 TRP A CD2 
1752 N  NE1 . TRP A 208 ? 0.0198 0.1025 0.1117 -0.0357 0.0108  -0.0390 208 TRP A NE1 
1753 C  CE2 . TRP A 208 ? 0.0307 0.1172 0.1005 -0.0519 0.0139  -0.0337 208 TRP A CE2 
1754 C  CE3 . TRP A 208 ? 0.0484 0.0982 0.1114 -0.0575 -0.0036 -0.0322 208 TRP A CE3 
1755 C  CZ2 . TRP A 208 ? 0.0466 0.1181 0.1249 -0.0657 -0.0014 -0.0199 208 TRP A CZ2 
1756 C  CZ3 . TRP A 208 ? 0.0397 0.1019 0.1245 -0.0458 -0.0211 -0.0296 208 TRP A CZ3 
1757 C  CH2 . TRP A 208 ? 0.0525 0.0827 0.1348 -0.0588 0.0111  -0.0274 208 TRP A CH2 
1758 N  N   . ILE A 209 ? 0.0121 0.1066 0.1168 -0.0240 0.0100  -0.0425 209 ILE A N   
1759 C  CA  . ILE A 209 ? 0.0163 0.1044 0.1423 -0.0312 0.0158  -0.0539 209 ILE A CA  
1760 C  C   . ILE A 209 ? 0.0097 0.1332 0.1308 -0.0206 0.0096  -0.0459 209 ILE A C   
1761 O  O   . ILE A 209 ? 0.0225 0.1177 0.1421 -0.0421 0.0069  -0.0325 209 ILE A O   
1762 C  CB  . ILE A 209 ? 0.0135 0.1142 0.1955 -0.0276 0.0139  -0.0661 209 ILE A CB  
1763 C  CG1 . ILE A 209 ? 0.0296 0.1269 0.2528 -0.0400 -0.0298 -0.0525 209 ILE A CG1 
1764 C  CG2 . ILE A 209 ? 0.0181 0.2048 0.2788 -0.0482 0.0201  -0.0976 209 ILE A CG2 
1765 C  CD1 . ILE A 209 ? 0.0439 0.1772 0.2915 -0.0779 0.0023  -0.0561 209 ILE A CD1 
1766 N  N   . VAL A 210 ? 0.0145 0.1122 0.1666 -0.0294 0.0108  -0.0387 210 VAL A N   
1767 C  CA  . VAL A 210 ? 0.0131 0.1112 0.1237 -0.0239 0.0030  -0.0591 210 VAL A CA  
1768 C  C   . VAL A 210 ? 0.0185 0.0925 0.1275 -0.0302 0.0237  -0.0309 210 VAL A C   
1769 O  O   . VAL A 210 ? 0.0148 0.1164 0.1355 -0.0303 0.0117  -0.0526 210 VAL A O   
1770 C  CB  . VAL A 210 ? 0.0147 0.1159 0.1667 -0.0302 0.0107  -0.0433 210 VAL A CB  
1771 C  CG1 . VAL A 210 ? 0.0104 0.1201 0.1629 -0.0185 -0.0044 -0.0467 210 VAL A CG1 
1772 C  CG2 . VAL A 210 ? 0.0171 0.1407 0.2040 -0.0368 0.0115  -0.0788 210 VAL A CG2 
1773 N  N   . LEU A 211 ? 0.0151 0.1094 0.1433 -0.0293 0.0178  -0.0376 211 LEU A N   
1774 C  CA  . LEU A 211 ? 0.0121 0.1340 0.1438 -0.0215 0.0235  -0.0422 211 LEU A CA  
1775 C  C   . LEU A 211 ? 0.0126 0.1351 0.1383 -0.0277 0.0143  -0.0500 211 LEU A C   
1776 O  O   . LEU A 211 ? 0.0182 0.1324 0.1350 -0.0378 0.0039  -0.0395 211 LEU A O   
1777 C  CB  . LEU A 211 ? 0.0217 0.1221 0.1635 -0.0399 0.0017  -0.0479 211 LEU A CB  
1778 C  CG  . LEU A 211 ? 0.0212 0.1239 0.1972 -0.0333 -0.0139 -0.0558 211 LEU A CG  
1779 C  CD1 . LEU A 211 ? 0.0350 0.1997 0.2146 -0.0621 -0.0273 -0.0438 211 LEU A CD1 
1780 C  CD2 . LEU A 211 ? 0.0305 0.1498 0.2063 -0.0583 0.0037  -0.0306 211 LEU A CD2 
1781 N  N   . LYS A 212 ? 0.0117 0.1362 0.1507 -0.0207 0.0234  -0.0411 212 LYS A N   
1782 C  CA  . LYS A 212 ? 0.0149 0.1581 0.1607 -0.0322 0.0271  -0.0566 212 LYS A CA  
1783 C  C   . LYS A 212 ? 0.0106 0.1097 0.1604 -0.0209 0.0142  -0.0788 212 LYS A C   
1784 O  O   . LYS A 212 ? 0.0414 0.1089 0.2031 -0.0210 -0.0247 -0.0793 212 LYS A O   
1785 C  CB  . LYS A 212 ? 0.0167 0.1994 0.1744 -0.0336 0.0344  -0.0723 212 LYS A CB  
1786 C  CG  . LYS A 212 ? 0.1388 0.2213 0.2476 0.0085  0.0104  -0.1071 212 LYS A CG  
1787 C  CD  . LYS A 212 ? 0.2246 0.2710 0.2500 -0.0050 0.0398  -0.0763 212 LYS A CD  
1788 C  CE  . LYS A 212 ? 0.2058 0.2868 0.3865 -0.0204 0.0820  -0.1472 212 LYS A CE  
1789 N  NZ  . LYS A 212 ? 0.2122 0.6697 0.4576 0.0710  0.1345  -0.0704 212 LYS A NZ  
1790 N  N   . GLU A 213 ? 0.0115 0.1231 0.1717 -0.0241 0.0161  -0.0528 213 GLU A N   
1791 C  CA  . GLU A 213 ? 0.0132 0.1269 0.1871 -0.0281 0.0200  -0.0550 213 GLU A CA  
1792 C  C   . GLU A 213 ? 0.0075 0.1087 0.1674 -0.0104 0.0011  -0.0502 213 GLU A C   
1793 O  O   . GLU A 213 ? 0.0125 0.1021 0.1836 -0.0187 -0.0047 -0.0479 213 GLU A O   
1794 C  CB  . GLU A 213 ? 0.0212 0.1720 0.2046 -0.0476 0.0257  -0.0370 213 GLU A CB  
1795 C  CG  . GLU A 213 ? 0.0555 0.1453 0.2521 -0.0145 -0.0017 -0.0381 213 GLU A CG  
1796 C  CD  . GLU A 213 ? 0.0429 0.2323 0.3389 0.0369  -0.0238 -0.0473 213 GLU A CD  
1797 O  OE1 . GLU A 213 ? 0.0127 0.2948 0.5914 -0.0358 -0.0355 0.0128  213 GLU A OE1 
1798 O  OE2 . GLU A 213 ? 0.2625 0.5621 0.4566 0.0023  -0.0190 0.1805  213 GLU A OE2 
1799 N  N   . PRO A 214 ? 0.0279 0.1091 0.1563 -0.0369 0.0042  -0.0517 214 PRO A N   
1800 C  CA  . PRO A 214 ? 0.0223 0.1383 0.1658 -0.0432 -0.0012 -0.0467 214 PRO A CA  
1801 C  C   . PRO A 214 ? 0.0305 0.1197 0.1720 -0.0473 -0.0043 -0.0495 214 PRO A C   
1802 O  O   . PRO A 214 ? 0.0178 0.1718 0.2120 -0.0201 -0.0161 -0.0552 214 PRO A O   
1803 C  CB  . PRO A 214 ? 0.0261 0.1212 0.1681 -0.0447 0.0001  -0.0365 214 PRO A CB  
1804 C  CG  . PRO A 214 ? 0.1089 0.1839 0.2304 -0.0154 0.0434  -0.0324 214 PRO A CG  
1805 C  CD  . PRO A 214 ? 0.0597 0.1142 0.1742 -0.0457 0.0250  -0.0564 214 PRO A CD  
1806 N  N   . ILE A 215 ? 0.0150 0.1406 0.1674 -0.0312 -0.0055 -0.0389 215 ILE A N   
1807 C  CA  . ILE A 215 ? 0.0254 0.1229 0.1579 -0.0447 -0.0059 -0.0281 215 ILE A CA  
1808 C  C   . ILE A 215 ? 0.0393 0.1186 0.1724 -0.0511 -0.0236 -0.0335 215 ILE A C   
1809 O  O   . ILE A 215 ? 0.0274 0.1279 0.1897 -0.0485 -0.0027 -0.0351 215 ILE A O   
1810 C  CB  . ILE A 215 ? 0.0575 0.1340 0.1693 -0.0628 -0.0189 -0.0318 215 ILE A CB  
1811 C  CG1 . ILE A 215 ? 0.0626 0.1327 0.1738 -0.0363 -0.0156 -0.0447 215 ILE A CG1 
1812 C  CG2 . ILE A 215 ? 0.0727 0.1295 0.1939 -0.0712 -0.0471 -0.0225 215 ILE A CG2 
1813 C  CD1 . ILE A 215 ? 0.1750 0.1306 0.1904 -0.0510 -0.0370 -0.0629 215 ILE A CD1 
1814 N  N   A SER A 216 ? 0.0479 0.1069 0.1753 -0.0465 -0.0179 -0.0255 216 SER A N   
1815 N  N   B SER A 216 ? 0.0420 0.1323 0.1901 -0.0403 -0.0129 -0.0209 216 SER A N   
1816 C  CA  A SER A 216 ? 0.0216 0.1215 0.1620 -0.0358 -0.0165 -0.0268 216 SER A CA  
1817 C  CA  B SER A 216 ? 0.0263 0.1780 0.1992 -0.0568 -0.0115 -0.0099 216 SER A CA  
1818 C  C   A SER A 216 ? 0.0290 0.0779 0.1735 -0.0257 -0.0286 -0.0418 216 SER A C   
1819 C  C   B SER A 216 ? 0.0268 0.1049 0.2157 -0.0370 -0.0179 -0.0366 216 SER A C   
1820 O  O   A SER A 216 ? 0.0351 0.0797 0.1625 -0.0244 -0.0223 -0.0574 216 SER A O   
1821 O  O   B SER A 216 ? 0.0111 0.1458 0.2117 -0.0171 -0.0165 -0.0478 216 SER A O   
1822 C  CB  A SER A 216 ? 0.0764 0.1590 0.1625 0.0183  0.0248  -0.0184 216 SER A CB  
1823 C  CB  B SER A 216 ? 0.1360 0.1771 0.2169 -0.0234 0.0011  -0.0447 216 SER A CB  
1824 O  OG  A SER A 216 ? 0.1523 0.1898 0.1759 0.0138  0.0179  -0.0312 216 SER A OG  
1825 O  OG  B SER A 216 ? 0.1249 0.2213 0.2211 -0.0149 -0.0009 -0.0272 216 SER A OG  
1826 N  N   . VAL A 217 ? 0.0490 0.1179 0.1488 -0.0173 -0.0042 -0.0380 217 VAL A N   
1827 C  CA  . VAL A 217 ? 0.0432 0.1168 0.1606 -0.0363 0.0038  -0.0337 217 VAL A CA  
1828 C  C   . VAL A 217 ? 0.0418 0.0996 0.1573 -0.0345 -0.0134 -0.0356 217 VAL A C   
1829 O  O   . VAL A 217 ? 0.0736 0.0985 0.1716 -0.0268 -0.0144 -0.0419 217 VAL A O   
1830 C  CB  . VAL A 217 ? 0.0451 0.1272 0.1835 -0.0290 -0.0255 -0.0323 217 VAL A CB  
1831 C  CG1 . VAL A 217 ? 0.0890 0.1021 0.1776 -0.0273 -0.0365 -0.0353 217 VAL A CG1 
1832 C  CG2 . VAL A 217 ? 0.0469 0.1261 0.2152 -0.0094 -0.0507 -0.0483 217 VAL A CG2 
1833 N  N   . SER A 218 ? 0.0763 0.1037 0.1541 -0.0261 -0.0078 -0.0301 218 SER A N   
1834 C  CA  . SER A 218 ? 0.0761 0.1091 0.1838 -0.0253 -0.0229 -0.0334 218 SER A CA  
1835 C  C   . SER A 218 ? 0.0663 0.1059 0.1706 -0.0221 -0.0203 -0.0468 218 SER A C   
1836 O  O   . SER A 218 ? 0.0649 0.1024 0.1703 -0.0334 -0.0096 -0.0351 218 SER A O   
1837 C  CB  . SER A 218 ? 0.0965 0.1550 0.1708 -0.0070 -0.0079 -0.0350 218 SER A CB  
1838 O  OG  . SER A 218 ? 0.1600 0.1256 0.1824 -0.0250 -0.0179 -0.0429 218 SER A OG  
1839 N  N   A SER A 219 ? 0.0888 0.1146 0.1876 -0.0252 -0.0111 -0.0286 219 SER A N   
1840 N  N   B SER A 219 ? 0.1203 0.1040 0.1965 -0.0266 -0.0188 -0.0452 219 SER A N   
1841 C  CA  A SER A 219 ? 0.1044 0.1225 0.1955 -0.0159 0.0171  -0.0400 219 SER A CA  
1842 C  CA  B SER A 219 ? 0.1427 0.1026 0.2108 -0.0170 0.0151  -0.0648 219 SER A CA  
1843 C  C   A SER A 219 ? 0.1667 0.1059 0.1955 -0.0099 0.0187  -0.0358 219 SER A C   
1844 C  C   B SER A 219 ? 0.1775 0.0815 0.2015 -0.0078 0.0103  -0.0508 219 SER A C   
1845 O  O   A SER A 219 ? 0.1625 0.1227 0.2034 -0.0081 0.0073  -0.0564 219 SER A O   
1846 O  O   B SER A 219 ? 0.1642 0.1424 0.2058 -0.0083 0.0179  -0.0615 219 SER A O   
1847 C  CB  A SER A 219 ? 0.0800 0.1220 0.1974 -0.0584 0.0326  -0.0017 219 SER A CB  
1848 C  CB  B SER A 219 ? 0.1913 0.0964 0.2924 -0.0126 -0.0032 -0.0877 219 SER A CB  
1849 O  OG  A SER A 219 ? 0.0921 0.1071 0.2042 -0.0609 -0.0024 -0.0311 219 SER A OG  
1850 O  OG  B SER A 219 ? 0.2025 0.2068 0.2556 -0.0266 0.0592  -0.0263 219 SER A OG  
1851 N  N   A GLU A 220 ? 0.1738 0.0987 0.1958 -0.0273 0.0129  -0.0356 220 GLU A N   
1852 N  N   B GLU A 220 ? 0.1553 0.1203 0.2095 -0.0131 0.0145  -0.0538 220 GLU A N   
1853 C  CA  A GLU A 220 ? 0.2156 0.1551 0.1714 0.0055  -0.0077 -0.0265 220 GLU A CA  
1854 C  CA  B GLU A 220 ? 0.2005 0.1409 0.1933 -0.0079 -0.0144 -0.0436 220 GLU A CA  
1855 C  C   A GLU A 220 ? 0.1963 0.1508 0.1249 -0.0047 -0.0107 -0.0425 220 GLU A C   
1856 C  C   B GLU A 220 ? 0.0985 0.1254 0.1536 -0.0505 -0.0238 -0.0670 220 GLU A C   
1857 O  O   A GLU A 220 ? 0.1952 0.1873 0.1596 -0.0049 -0.0065 -0.0477 220 GLU A O   
1858 O  O   B GLU A 220 ? 0.2282 0.1502 0.1481 -0.0119 0.0201  -0.0578 220 GLU A O   
1859 C  CB  A GLU A 220 ? 0.1961 0.1550 0.2307 0.0107  -0.0322 -0.0107 220 GLU A CB  
1860 C  CB  B GLU A 220 ? 0.2569 0.1946 0.2244 -0.0106 -0.0769 -0.0702 220 GLU A CB  
1861 C  CG  A GLU A 220 ? 0.2133 0.1588 0.2600 -0.0025 -0.0212 0.0121  220 GLU A CG  
1862 C  CG  B GLU A 220 ? 0.3259 0.1818 0.3276 -0.0256 -0.0513 -0.0841 220 GLU A CG  
1863 C  CD  A GLU A 220 ? 0.2257 0.1540 0.2856 0.0287  0.0034  0.0479  220 GLU A CD  
1864 C  CD  B GLU A 220 ? 0.4017 0.2904 0.3970 0.0242  0.0263  -0.0854 220 GLU A CD  
1865 O  OE1 A GLU A 220 ? 0.1123 0.1418 0.2285 -0.0001 -0.0420 -0.0174 220 GLU A OE1 
1866 O  OE1 B GLU A 220 ? 0.3433 0.2016 0.4332 0.0482  -0.0245 -0.0013 220 GLU A OE1 
1867 O  OE2 A GLU A 220 ? 0.3033 0.1518 0.3094 0.0607  0.0002  0.0223  220 GLU A OE2 
1868 O  OE2 B GLU A 220 ? 0.4474 0.4750 0.5274 0.0022  0.0627  -0.0537 220 GLU A OE2 
1869 N  N   . GLN A 221 ? 0.1376 0.1100 0.1537 -0.0166 -0.0278 -0.0522 221 GLN A N   
1870 C  CA  . GLN A 221 ? 0.1230 0.1109 0.1642 -0.0006 -0.0287 -0.0747 221 GLN A CA  
1871 C  C   . GLN A 221 ? 0.0974 0.1077 0.1802 -0.0291 -0.0145 -0.0539 221 GLN A C   
1872 O  O   . GLN A 221 ? 0.1556 0.1104 0.1694 -0.0023 0.0021  -0.0433 221 GLN A O   
1873 C  CB  . GLN A 221 ? 0.1421 0.1599 0.1582 -0.0046 -0.0375 -0.0179 221 GLN A CB  
1874 C  CG  . GLN A 221 ? 0.1428 0.1304 0.1585 -0.0107 -0.0478 -0.0228 221 GLN A CG  
1875 C  CD  . GLN A 221 ? 0.1717 0.0987 0.1810 -0.0223 -0.0616 -0.0229 221 GLN A CD  
1876 O  OE1 . GLN A 221 ? 0.1405 0.1371 0.1646 -0.0398 -0.0368 -0.0285 221 GLN A OE1 
1877 N  NE2 . GLN A 221 ? 0.1222 0.1421 0.1978 -0.0331 -0.0510 -0.0400 221 GLN A NE2 
1878 N  N   A VAL A 222 ? 0.1326 0.0952 0.1676 -0.0243 -0.0066 -0.0582 222 VAL A N   
1879 N  N   B VAL A 222 ? 0.1358 0.1142 0.1705 -0.0356 -0.0096 -0.0615 222 VAL A N   
1880 C  CA  A VAL A 222 ? 0.1087 0.0957 0.1641 -0.0428 0.0027  -0.0555 222 VAL A CA  
1881 C  CA  B VAL A 222 ? 0.1120 0.1495 0.1766 -0.0517 0.0027  -0.0462 222 VAL A CA  
1882 C  C   A VAL A 222 ? 0.1309 0.1428 0.1753 -0.0190 0.0304  -0.0521 222 VAL A C   
1883 C  C   B VAL A 222 ? 0.0996 0.1555 0.1715 -0.0229 0.0046  -0.0510 222 VAL A C   
1884 O  O   A VAL A 222 ? 0.1361 0.1211 0.1761 -0.0255 0.0159  -0.0672 222 VAL A O   
1885 O  O   B VAL A 222 ? 0.0983 0.1384 0.2052 -0.0309 -0.0199 -0.0560 222 VAL A O   
1886 C  CB  A VAL A 222 ? 0.0942 0.1076 0.1612 -0.0436 0.0158  -0.0508 222 VAL A CB  
1887 C  CB  B VAL A 222 ? 0.0958 0.2070 0.1914 -0.0601 0.0269  -0.0761 222 VAL A CB  
1888 C  CG1 A VAL A 222 ? 0.0176 0.1068 0.1978 -0.0255 -0.0058 -0.0765 222 VAL A CG1 
1889 C  CG1 B VAL A 222 ? 0.1118 0.2741 0.1861 -0.0801 -0.0044 -0.0480 222 VAL A CG1 
1890 C  CG2 A VAL A 222 ? 0.0750 0.1233 0.1777 -0.0528 0.0186  -0.0352 222 VAL A CG2 
1891 C  CG2 B VAL A 222 ? 0.0076 0.2335 0.1884 -0.0084 0.0148  -0.0636 222 VAL A CG2 
1892 N  N   . LEU A 223 ? 0.1547 0.1276 0.1916 -0.0038 0.0420  -0.0474 223 LEU A N   
1893 C  CA  . LEU A 223 ? 0.1593 0.1252 0.2365 -0.0265 0.0453  -0.0508 223 LEU A CA  
1894 C  C   . LEU A 223 ? 0.1243 0.1381 0.2031 -0.0075 0.0354  -0.0398 223 LEU A C   
1895 O  O   . LEU A 223 ? 0.1134 0.1954 0.2011 0.0192  0.0281  -0.0310 223 LEU A O   
1896 C  CB  . LEU A 223 ? 0.2000 0.1500 0.2815 0.0173  0.0820  -0.0080 223 LEU A CB  
1897 C  CG  . LEU A 223 ? 0.3977 0.1913 0.3690 0.0167  0.0776  -0.0776 223 LEU A CG  
1898 C  CD1 . LEU A 223 ? 0.2698 0.2219 0.4737 -0.1171 -0.0373 -0.0396 223 LEU A CD1 
1899 C  CD2 . LEU A 223 ? 0.3931 0.2714 0.4552 0.0682  0.1680  -0.0230 223 LEU A CD2 
1900 N  N   . LYS A 224 ? 0.1536 0.1447 0.1931 -0.0168 0.0215  -0.0435 224 LYS A N   
1901 C  CA  . LYS A 224 ? 0.2670 0.1879 0.1728 0.0310  0.0318  -0.0527 224 LYS A CA  
1902 C  C   . LYS A 224 ? 0.1150 0.1846 0.1557 -0.0230 0.0272  -0.0365 224 LYS A C   
1903 O  O   . LYS A 224 ? 0.2001 0.1577 0.1462 0.0200  0.0118  -0.0559 224 LYS A O   
1904 C  CB  . LYS A 224 ? 0.2696 0.3310 0.1894 0.0526  -0.0066 -0.0877 224 LYS A CB  
1905 C  CG  . LYS A 224 ? 0.2926 0.3197 0.2512 0.0166  -0.0160 -0.0489 224 LYS A CG  
1906 C  CD  . LYS A 224 ? 0.4432 0.5344 0.2990 -0.0092 -0.1773 -0.0522 224 LYS A CD  
1907 C  CE  . LYS A 224 ? 0.6692 0.6059 0.4490 0.1031  0.0016  0.0145  224 LYS A CE  
1908 N  NZ  . LYS A 224 ? 0.6369 0.5725 0.3421 0.1671  0.2233  -0.0228 224 LYS A NZ  
1909 N  N   . PHE A 225 ? 0.1625 0.1388 0.1393 0.0096  0.0303  -0.0293 225 PHE A N   
1910 C  CA  . PHE A 225 ? 0.1384 0.1418 0.1500 -0.0051 0.0361  -0.0505 225 PHE A CA  
1911 C  C   . PHE A 225 ? 0.1541 0.1327 0.1475 0.0044  0.0291  -0.0468 225 PHE A C   
1912 O  O   . PHE A 225 ? 0.1712 0.1525 0.1439 0.0206  0.0358  -0.0325 225 PHE A O   
1913 C  CB  . PHE A 225 ? 0.1477 0.1246 0.1460 -0.0352 0.0400  -0.0383 225 PHE A CB  
1914 C  CG  . PHE A 225 ? 0.0958 0.1207 0.1856 -0.0271 0.0122  -0.0245 225 PHE A CG  
1915 C  CD1 . PHE A 225 ? 0.1438 0.1384 0.2120 -0.0396 0.0138  -0.0625 225 PHE A CD1 
1916 C  CD2 . PHE A 225 ? 0.1130 0.1661 0.1746 -0.0122 0.0175  -0.0198 225 PHE A CD2 
1917 C  CE1 . PHE A 225 ? 0.1988 0.1521 0.2149 -0.0508 0.0373  -0.0451 225 PHE A CE1 
1918 C  CE2 . PHE A 225 ? 0.0757 0.2202 0.2070 -0.0271 -0.0182 0.0047  225 PHE A CE2 
1919 C  CZ  . PHE A 225 ? 0.0902 0.1408 0.2167 -0.0280 0.0257  -0.0249 225 PHE A CZ  
1920 N  N   . ARG A 226 ? 0.1418 0.1307 0.1273 -0.0171 0.0111  -0.0458 226 ARG A N   
1921 C  CA  . ARG A 226 ? 0.1308 0.1494 0.1409 -0.0223 0.0021  -0.0530 226 ARG A CA  
1922 C  C   . ARG A 226 ? 0.1759 0.1588 0.1664 0.0347  0.0266  -0.0461 226 ARG A C   
1923 O  O   . ARG A 226 ? 0.1823 0.2042 0.1782 0.0240  0.0573  -0.0275 226 ARG A O   
1924 C  CB  . ARG A 226 ? 0.0922 0.1444 0.1626 0.0020  0.0530  -0.0392 226 ARG A CB  
1925 C  CG  . ARG A 226 ? 0.1456 0.1473 0.1577 -0.0003 0.0442  -0.0364 226 ARG A CG  
1926 C  CD  . ARG A 226 ? 0.2593 0.1641 0.1476 -0.0312 0.0287  -0.0682 226 ARG A CD  
1927 N  NE  . ARG A 226 ? 0.1057 0.1459 0.1600 -0.0228 0.0132  -0.0435 226 ARG A NE  
1928 C  CZ  . ARG A 226 ? 0.1080 0.1509 0.1488 -0.0133 -0.0144 -0.0451 226 ARG A CZ  
1929 N  NH1 . ARG A 226 ? 0.2106 0.2071 0.1697 0.0449  -0.0015 0.0055  226 ARG A NH1 
1930 N  NH2 . ARG A 226 ? 0.1245 0.1469 0.1676 -0.0249 0.0232  -0.0359 226 ARG A NH2 
1931 N  N   . LYS A 227 ? 0.1428 0.1430 0.1535 0.0285  0.0323  -0.0204 227 LYS A N   
1932 C  CA  . LYS A 227 ? 0.2119 0.1881 0.1729 0.0551  0.0646  -0.0027 227 LYS A CA  
1933 C  C   . LYS A 227 ? 0.2912 0.1993 0.1252 0.0683  0.0430  -0.0287 227 LYS A C   
1934 O  O   . LYS A 227 ? 0.2648 0.2480 0.1353 0.0894  0.0457  -0.0302 227 LYS A O   
1935 C  CB  . LYS A 227 ? 0.2355 0.1562 0.1717 0.0012  0.0275  -0.0167 227 LYS A CB  
1936 C  CG  . LYS A 227 ? 0.2992 0.1890 0.2567 0.0428  -0.0190 -0.0245 227 LYS A CG  
1937 C  CD  . LYS A 227 ? 0.2282 0.3480 0.3168 0.0374  -0.0064 -0.0034 227 LYS A CD  
1938 C  CE  . LYS A 227 ? 0.3213 0.4655 0.3759 0.0769  0.0397  0.1109  227 LYS A CE  
1939 N  NZ  . LYS A 227 ? 0.7307 0.6010 0.5252 0.2306  -0.1438 0.1474  227 LYS A NZ  
1940 N  N   . LEU A 228 ? 0.2349 0.1539 0.1348 0.0288  0.0277  -0.0391 228 LEU A N   
1941 C  CA  . LEU A 228 ? 0.2850 0.1861 0.1276 0.0869  -0.0002 -0.0528 228 LEU A CA  
1942 C  C   . LEU A 228 ? 0.2850 0.2179 0.1489 0.1000  0.0391  -0.0129 228 LEU A C   
1943 O  O   . LEU A 228 ? 0.2492 0.1842 0.1535 0.0893  0.0612  -0.0284 228 LEU A O   
1944 C  CB  . LEU A 228 ? 0.3104 0.1970 0.1290 0.0805  -0.0062 -0.0275 228 LEU A CB  
1945 C  CG  . LEU A 228 ? 0.2606 0.1886 0.1281 0.0882  0.0017  -0.0591 228 LEU A CG  
1946 C  CD1 . LEU A 228 ? 0.2136 0.1500 0.1986 0.0318  -0.0024 -0.0427 228 LEU A CD1 
1947 C  CD2 . LEU A 228 ? 0.3077 0.1708 0.1533 -0.0010 0.0046  -0.0650 228 LEU A CD2 
1948 N  N   A ASN A 229 ? 0.3609 0.2333 0.2129 0.1460  0.0276  -0.0127 229 ASN A N   
1949 N  N   B ASN A 229 ? 0.3602 0.2323 0.2150 0.1460  0.0252  -0.0107 229 ASN A N   
1950 C  CA  A ASN A 229 ? 0.3776 0.2955 0.1342 0.1391  0.1052  -0.0060 229 ASN A CA  
1951 C  CA  B ASN A 229 ? 0.3800 0.2976 0.1331 0.1370  0.1018  -0.0032 229 ASN A CA  
1952 C  C   A ASN A 229 ? 0.3242 0.3173 0.1802 0.1033  0.0485  0.0316  229 ASN A C   
1953 C  C   B ASN A 229 ? 0.3207 0.3175 0.1760 0.1045  0.0530  0.0309  229 ASN A C   
1954 O  O   A ASN A 229 ? 0.3459 0.2606 0.1628 0.1427  0.0727  -0.0138 229 ASN A O   
1955 O  O   B ASN A 229 ? 0.3470 0.2614 0.1630 0.1412  0.0724  -0.0127 229 ASN A O   
1956 C  CB  A ASN A 229 ? 0.4603 0.3328 0.1485 0.1266  0.1432  -0.0044 229 ASN A CB  
1957 C  CB  B ASN A 229 ? 0.4641 0.3292 0.1489 0.1184  0.1404  -0.0113 229 ASN A CB  
1958 C  CG  A ASN A 229 ? 0.4109 0.3202 0.1847 0.1470  0.1280  0.0038  229 ASN A CG  
1959 C  CG  B ASN A 229 ? 0.4289 0.2957 0.1679 0.1673  0.1018  -0.0138 229 ASN A CG  
1960 O  OD1 A ASN A 229 ? 0.5814 0.3874 0.1580 0.1448  0.0778  -0.0097 229 ASN A OD1 
1961 O  OD1 B ASN A 229 ? 0.5001 0.3648 0.1371 0.1822  0.1098  -0.0223 229 ASN A OD1 
1962 N  ND2 A ASN A 229 ? 0.3393 0.3014 0.2052 0.1219  0.1070  0.0170  229 ASN A ND2 
1963 N  ND2 B ASN A 229 ? 0.3221 0.3060 0.2039 0.1346  0.1146  0.0190  229 ASN A ND2 
1964 N  N   . PHE A 230 ? 0.2594 0.2873 0.1407 0.1333  0.1050  -0.0170 230 PHE A N   
1965 C  CA  . PHE A 230 ? 0.3335 0.2687 0.1702 0.1537  0.1293  0.0071  230 PHE A CA  
1966 C  C   . PHE A 230 ? 0.2669 0.2565 0.2311 0.1075  0.1283  -0.0342 230 PHE A C   
1967 O  O   . PHE A 230 ? 0.2882 0.2759 0.1957 0.1207  0.0813  -0.0130 230 PHE A O   
1968 C  CB  . PHE A 230 ? 0.3257 0.3028 0.1767 0.1608  0.1147  0.0271  230 PHE A CB  
1969 C  CG  . PHE A 230 ? 0.2604 0.2865 0.2081 0.1525  0.1226  0.0130  230 PHE A CG  
1970 C  CD1 . PHE A 230 ? 0.2484 0.2468 0.1665 0.1234  0.0700  -0.0049 230 PHE A CD1 
1971 C  CD2 . PHE A 230 ? 0.2592 0.2737 0.1834 0.1391  0.0829  0.0151  230 PHE A CD2 
1972 C  CE1 . PHE A 230 ? 0.2303 0.2535 0.1923 0.1323  0.0861  0.0012  230 PHE A CE1 
1973 C  CE2 . PHE A 230 ? 0.2860 0.2447 0.1763 0.1239  0.0898  0.0211  230 PHE A CE2 
1974 C  CZ  . PHE A 230 ? 0.1692 0.2532 0.1580 0.1307  0.0506  -0.0021 230 PHE A CZ  
1975 N  N   A ASN A 231 ? 0.3863 0.3221 0.2258 0.1316  0.1117  0.0263  231 ASN A N   
1976 N  N   B ASN A 231 ? 0.3112 0.3067 0.1653 0.2233  0.1467  -0.0013 231 ASN A N   
1977 C  CA  A ASN A 231 ? 0.4262 0.2969 0.2723 0.0451  0.2183  0.0443  231 ASN A CA  
1978 C  CA  B ASN A 231 ? 0.2930 0.3078 0.1849 0.1964  0.1687  0.0020  231 ASN A CA  
1979 C  C   A ASN A 231 ? 0.4591 0.3137 0.3678 0.0506  0.2433  -0.0440 231 ASN A C   
1980 C  C   B ASN A 231 ? 0.4562 0.2388 0.1847 0.1595  0.1192  0.0342  231 ASN A C   
1981 O  O   A ASN A 231 ? 0.8758 6.4822 1.6957 -0.2035 1.1425  0.8318  231 ASN A O   
1982 O  O   B ASN A 231 ? 0.4482 0.2050 0.0852 0.1813  0.1065  -0.0013 231 ASN A O   
1983 C  CB  A ASN A 231 ? 0.0955 0.1783 0.4892 -0.1235 0.0964  -0.1166 231 ASN A CB  
1984 C  CB  B ASN A 231 ? 0.3107 0.3165 0.1275 0.1527  0.0776  0.0037  231 ASN A CB  
1985 C  CG  A ASN A 231 ? 0.0507 0.2243 0.2714 -0.0967 0.0659  -0.1094 231 ASN A CG  
1986 C  CG  B ASN A 231 ? 0.0269 0.1673 0.1887 -0.0278 -0.0085 -0.0397 231 ASN A CG  
1987 O  OD1 A ASN A 231 ? 0.0666 0.1652 0.2766 -0.0978 0.0488  -0.0759 231 ASN A OD1 
1988 O  OD1 B ASN A 231 ? 0.1309 0.2122 0.1878 -0.0403 -0.0083 0.0146  231 ASN A OD1 
1989 N  ND2 A ASN A 231 ? 0.0927 0.2013 0.2243 -0.1159 0.1077  -0.0871 231 ASN A ND2 
1990 N  ND2 B ASN A 231 ? 0.0502 0.0779 0.2120 -0.0528 -0.0115 -0.0265 231 ASN A ND2 
1991 N  N   . GLY A 232 ? 0.5334 0.2144 0.2870 0.1596  0.1151  0.0010  232 GLY A N   
1992 C  CA  . GLY A 232 ? 0.5583 0.2777 0.2855 0.1126  0.1464  -0.0156 232 GLY A CA  
1993 C  C   . GLY A 232 ? 0.1269 0.2173 0.3133 0.0265  -0.0513 -0.0885 232 GLY A C   
1994 O  O   . GLY A 232 ? 0.1567 0.2823 0.4330 -0.0979 0.1112  0.0092  232 GLY A O   
1995 N  N   . GLU A 233 ? 0.1694 0.2873 0.2255 0.0075  -0.0006 -0.0831 233 GLU A N   
1996 C  CA  . GLU A 233 ? 0.1457 0.2298 0.2714 0.0322  -0.0245 -0.0788 233 GLU A CA  
1997 C  C   . GLU A 233 ? 0.2160 0.3082 0.3805 -0.0611 0.0803  -0.1737 233 GLU A C   
1998 O  O   . GLU A 233 ? 0.1881 0.3166 0.2865 -0.0895 0.0648  -0.1456 233 GLU A O   
1999 C  CB  . GLU A 233 ? 0.1877 0.2945 0.2422 -0.0240 -0.0196 -0.0511 233 GLU A CB  
2000 C  CG  . GLU A 233 ? 0.1059 0.4090 0.2052 0.0237  0.0210  -0.0620 233 GLU A CG  
2001 C  CD  . GLU A 233 ? 0.4820 0.4205 0.3787 -0.0126 -0.1136 -0.0630 233 GLU A CD  
2002 O  OE1 . GLU A 233 ? 0.3781 0.4031 0.3656 0.0837  0.1705  -0.0427 233 GLU A OE1 
2003 O  OE2 . GLU A 233 ? 0.4336 0.5464 0.5034 0.0699  -0.1940 0.0504  233 GLU A OE2 
2004 N  N   . GLY A 234 ? 0.3253 0.3823 0.6236 -0.2186 0.1421  -0.0126 234 GLY A N   
2005 C  CA  . GLY A 234 ? 0.2587 0.2454 0.7531 -0.0476 0.2358  0.1074  234 GLY A CA  
2006 C  C   . GLY A 234 ? 0.6335 0.5323 0.7669 -0.0060 0.0767  -0.0485 234 GLY A C   
2007 O  O   . GLY A 234 ? 1.1970 0.4204 0.5656 0.1948  0.6072  0.0756  234 GLY A O   
2008 N  N   . GLU A 235 ? 0.9173 0.4041 0.5291 0.0597  0.1024  -0.0120 235 GLU A N   
2009 C  CA  . GLU A 235 ? 1.0892 0.3430 0.4035 0.0913  0.0648  -0.0419 235 GLU A CA  
2010 C  C   . GLU A 235 ? 0.1229 0.3001 0.2680 -0.1187 0.0407  -0.0107 235 GLU A C   
2011 O  O   . GLU A 235 ? 0.1472 0.4535 0.2367 -0.0573 0.0164  -0.1018 235 GLU A O   
2012 C  CB  . GLU A 235 ? 1.2545 0.4662 0.4484 0.1502  0.2680  0.0663  235 GLU A CB  
2013 C  CG  . GLU A 235 ? 1.1354 0.4161 0.7221 -0.0376 0.2411  0.0512  235 GLU A CG  
2014 C  CD  . GLU A 235 ? 0.8784 0.6876 0.5121 -0.2466 -0.0079 0.0228  235 GLU A CD  
2015 O  OE1 . GLU A 235 ? 0.3272 0.4863 0.4565 -0.0207 -0.0604 0.0617  235 GLU A OE1 
2016 O  OE2 . GLU A 235 ? 0.8313 0.5570 0.8126 -0.3119 -0.0317 0.2349  235 GLU A OE2 
2017 N  N   . PRO A 236 ? 0.1208 0.3283 0.3367 -0.0103 -0.0304 -0.0719 236 PRO A N   
2018 C  CA  . PRO A 236 ? 0.1109 0.2645 0.3191 -0.1428 0.1147  -0.1242 236 PRO A CA  
2019 C  C   . PRO A 236 ? 0.0861 0.2569 0.2362 -0.0889 0.0435  -0.0971 236 PRO A C   
2020 O  O   . PRO A 236 ? 0.2581 0.2721 0.2771 0.0057  0.1732  -0.0137 236 PRO A O   
2021 C  CB  . PRO A 236 ? 0.1621 0.2532 0.2855 -0.1106 0.0814  -0.1072 236 PRO A CB  
2022 C  CG  . PRO A 236 ? 0.1145 0.3389 0.3472 -0.0973 0.0817  -0.0969 236 PRO A CG  
2023 C  CD  . PRO A 236 ? 0.0787 0.4177 0.3683 -0.1395 -0.0082 -0.1367 236 PRO A CD  
2024 N  N   . GLU A 237 ? 0.2748 0.5073 0.2113 0.1417  0.1236  0.0193  237 GLU A N   
2025 C  CA  . GLU A 237 ? 0.2552 0.3910 0.2387 0.1405  0.0841  -0.0036 237 GLU A CA  
2026 C  C   . GLU A 237 ? 0.3507 0.3023 0.2375 0.1937  0.1043  0.0250  237 GLU A C   
2027 O  O   . GLU A 237 ? 0.2212 0.3886 0.2535 0.1294  0.1222  0.0616  237 GLU A O   
2028 C  CB  . GLU A 237 ? 0.3719 0.4319 0.2061 0.2130  0.0556  -0.0406 237 GLU A CB  
2029 C  CG  . GLU A 237 ? 0.2836 0.3028 0.4060 0.0526  0.0111  -0.0016 237 GLU A CG  
2030 C  CD  . GLU A 237 ? 0.4070 0.5253 0.3732 0.0644  0.0201  0.0439  237 GLU A CD  
2031 O  OE1 . GLU A 237 ? 0.0924 0.7426 0.4297 0.0258  0.0206  0.1185  237 GLU A OE1 
2032 O  OE2 . GLU A 237 ? 0.3725 0.4278 0.2517 0.1380  0.0416  0.0039  237 GLU A OE2 
2033 N  N   . GLU A 238 ? 0.3510 0.3686 0.2098 0.1869  0.1229  0.0406  238 GLU A N   
2034 C  CA  . GLU A 238 ? 0.1557 0.4475 0.2263 0.1204  0.0813  0.0000  238 GLU A CA  
2035 C  C   . GLU A 238 ? 0.1518 0.3745 0.2493 0.1353  0.0678  0.0023  238 GLU A C   
2036 O  O   . GLU A 238 ? 0.2142 0.3077 0.1801 0.1181  0.0512  -0.0389 238 GLU A O   
2037 C  CB  . GLU A 238 ? 0.0359 0.2992 0.3633 -0.0855 0.0087  -0.0057 238 GLU A CB  
2038 C  CG  . GLU A 238 ? 0.0245 0.3685 0.4325 -0.0433 0.0688  0.0006  238 GLU A CG  
2039 C  CD  . GLU A 238 ? 0.1689 0.2617 0.3367 -0.0905 0.0558  0.0329  238 GLU A CD  
2040 O  OE1 . GLU A 238 ? 0.2287 0.5211 0.3521 -0.0077 0.0976  -0.0284 238 GLU A OE1 
2041 O  OE2 . GLU A 238 ? 0.2157 0.6092 0.3717 0.1850  0.0181  -0.0506 238 GLU A OE2 
2042 N  N   . LEU A 239 ? 0.1450 0.3145 0.1675 0.0932  0.0798  0.0059  239 LEU A N   
2043 C  CA  . LEU A 239 ? 0.1326 0.2323 0.1586 0.0635  0.0788  -0.0142 239 LEU A CA  
2044 C  C   . LEU A 239 ? 0.1546 0.2548 0.1292 0.0734  0.0763  -0.0154 239 LEU A C   
2045 O  O   . LEU A 239 ? 0.1097 0.2400 0.1796 0.0402  0.0675  -0.0121 239 LEU A O   
2046 C  CB  . LEU A 239 ? 0.1560 0.1690 0.1709 -0.0048 0.0605  -0.0391 239 LEU A CB  
2047 C  CG  . LEU A 239 ? 0.0365 0.1863 0.2333 -0.0723 0.0272  -0.0293 239 LEU A CG  
2048 C  CD1 . LEU A 239 ? 0.1415 0.1479 0.4135 -0.0639 -0.0093 -0.0289 239 LEU A CD1 
2049 C  CD2 . LEU A 239 ? 0.0457 0.2377 0.2504 -0.0938 0.0352  -0.0435 239 LEU A CD2 
2050 N  N   . MET A 240 ? 0.2002 0.1744 0.1409 0.0594  0.0710  -0.0187 240 MET A N   
2051 C  CA  . MET A 240 ? 0.2216 0.1962 0.1433 0.0367  0.0996  -0.0412 240 MET A CA  
2052 C  C   . MET A 240 ? 0.1476 0.1567 0.1419 0.0553  0.0636  -0.0201 240 MET A C   
2053 O  O   . MET A 240 ? 0.1324 0.1620 0.1421 0.0225  0.0379  -0.0494 240 MET A O   
2054 C  CB  . MET A 240 ? 0.2572 0.1823 0.1323 0.0538  0.0880  -0.0374 240 MET A CB  
2055 C  CG  . MET A 240 ? 0.2117 0.1898 0.1441 0.0725  0.0771  -0.0187 240 MET A CG  
2056 S  SD  . MET A 240 ? 0.2897 0.1574 0.1641 0.0601  0.0502  -0.0482 240 MET A SD  
2057 C  CE  . MET A 240 ? 0.2829 0.1676 0.1496 0.0656  0.0825  -0.0368 240 MET A CE  
2058 N  N   . VAL A 241 ? 0.1286 0.1478 0.1412 0.0234  0.0736  -0.0172 241 VAL A N   
2059 C  CA  . VAL A 241 ? 0.1122 0.1236 0.1209 -0.0038 0.0562  -0.0214 241 VAL A CA  
2060 C  C   . VAL A 241 ? 0.0326 0.1195 0.1593 -0.0137 0.0627  -0.0144 241 VAL A C   
2061 O  O   . VAL A 241 ? 0.0387 0.1474 0.1639 0.0017  0.0529  -0.0233 241 VAL A O   
2062 C  CB  . VAL A 241 ? 0.0757 0.1254 0.1593 -0.0067 0.0436  -0.0145 241 VAL A CB  
2063 C  CG1 . VAL A 241 ? 0.0906 0.1527 0.1688 0.0042  0.0504  -0.0223 241 VAL A CG1 
2064 C  CG2 . VAL A 241 ? 0.0947 0.1300 0.2075 -0.0006 0.0656  -0.0044 241 VAL A CG2 
2065 N  N   . ASP A 242 ? 0.0714 0.0955 0.1326 -0.0013 0.0490  -0.0275 242 ASP A N   
2066 C  CA  . ASP A 242 ? 0.0703 0.1071 0.1483 -0.0392 0.0518  -0.0273 242 ASP A CA  
2067 C  C   . ASP A 242 ? 0.0477 0.1113 0.1555 -0.0099 0.0584  -0.0212 242 ASP A C   
2068 O  O   . ASP A 242 ? 0.0432 0.1351 0.1962 -0.0131 0.0460  -0.0106 242 ASP A O   
2069 C  CB  . ASP A 242 ? 0.0753 0.1058 0.1694 -0.0359 0.0432  -0.0288 242 ASP A CB  
2070 C  CG  . ASP A 242 ? 0.0353 0.1185 0.1522 -0.0351 0.0396  -0.0284 242 ASP A CG  
2071 O  OD1 . ASP A 242 ? 0.0342 0.1034 0.1632 -0.0266 0.0419  -0.0194 242 ASP A OD1 
2072 O  OD2 . ASP A 242 ? 0.0415 0.1427 0.1832 -0.0418 0.0505  -0.0130 242 ASP A OD2 
2073 N  N   . ASN A 243 ? 0.0428 0.1091 0.1301 -0.0119 0.0602  -0.0173 243 ASN A N   
2074 C  CA  . ASN A 243 ? 0.0345 0.1082 0.1538 -0.0159 0.0634  -0.0319 243 ASN A CA  
2075 C  C   . ASN A 243 ? 0.0549 0.1091 0.1286 0.0010  0.0439  -0.0278 243 ASN A C   
2076 O  O   . ASN A 243 ? 0.0750 0.1098 0.1384 -0.0225 0.0473  -0.0297 243 ASN A O   
2077 C  CB  . ASN A 243 ? 0.0512 0.1350 0.1384 -0.0069 0.0579  -0.0348 243 ASN A CB  
2078 C  CG  . ASN A 243 ? 0.0646 0.1277 0.1285 0.0064  0.0458  -0.0273 243 ASN A CG  
2079 O  OD1 . ASN A 243 ? 0.0669 0.1166 0.1580 -0.0059 0.0296  -0.0531 243 ASN A OD1 
2080 N  ND2 . ASN A 243 ? 0.1052 0.1637 0.1443 0.0227  0.0111  -0.0633 243 ASN A ND2 
2081 N  N   . TRP A 244 ? 0.0284 0.0991 0.1328 -0.0208 0.0396  -0.0340 244 TRP A N   
2082 C  CA  . TRP A 244 ? 0.0176 0.0839 0.1302 -0.0287 0.0198  -0.0308 244 TRP A CA  
2083 C  C   . TRP A 244 ? 0.0191 0.0886 0.1394 -0.0320 0.0194  -0.0353 244 TRP A C   
2084 O  O   . TRP A 244 ? 0.0235 0.1222 0.1775 -0.0445 0.0125  -0.0234 244 TRP A O   
2085 C  CB  . TRP A 244 ? 0.0151 0.0965 0.1571 -0.0271 0.0219  -0.0406 244 TRP A CB  
2086 C  CG  . TRP A 244 ? 0.0120 0.0853 0.1312 -0.0193 0.0190  -0.0371 244 TRP A CG  
2087 C  CD1 . TRP A 244 ? 0.0118 0.1038 0.1254 -0.0230 0.0149  -0.0515 244 TRP A CD1 
2088 C  CD2 . TRP A 244 ? 0.0161 0.0824 0.1257 -0.0227 0.0290  -0.0404 244 TRP A CD2 
2089 N  NE1 . TRP A 244 ? 0.0212 0.0967 0.1358 -0.0307 0.0350  -0.0390 244 TRP A NE1 
2090 C  CE2 . TRP A 244 ? 0.0177 0.0922 0.1393 -0.0281 0.0272  -0.0345 244 TRP A CE2 
2091 C  CE3 . TRP A 244 ? 0.0251 0.1109 0.1350 -0.0441 0.0261  -0.0521 244 TRP A CE3 
2092 C  CZ2 . TRP A 244 ? 0.0454 0.0963 0.1498 -0.0401 0.0040  -0.0300 244 TRP A CZ2 
2093 C  CZ3 . TRP A 244 ? 0.0333 0.1151 0.1547 -0.0540 0.0235  -0.0533 244 TRP A CZ3 
2094 C  CH2 . TRP A 244 ? 0.0273 0.1187 0.1662 -0.0454 0.0007  -0.0482 244 TRP A CH2 
2095 N  N   . ARG A 245 ? 0.0139 0.1114 0.1171 -0.0211 0.0234  -0.0241 245 ARG A N   
2096 C  CA  . ARG A 245 ? 0.0188 0.1219 0.1460 -0.0347 0.0239  -0.0250 245 ARG A CA  
2097 C  C   . ARG A 245 ? 0.0275 0.1279 0.1401 -0.0508 0.0149  -0.0407 245 ARG A C   
2098 O  O   . ARG A 245 ? 0.0213 0.1360 0.1553 -0.0428 0.0219  -0.0344 245 ARG A O   
2099 C  CB  . ARG A 245 ? 0.0147 0.1348 0.1403 -0.0326 0.0073  -0.0185 245 ARG A CB  
2100 C  CG  . ARG A 245 ? 0.0077 0.1639 0.1571 -0.0146 0.0037  -0.0176 245 ARG A CG  
2101 C  CD  . ARG A 245 ? 0.0089 0.1775 0.1998 -0.0196 0.0095  -0.0157 245 ARG A CD  
2102 N  NE  . ARG A 245 ? 0.0097 0.1609 0.1991 -0.0228 0.0011  -0.0253 245 ARG A NE  
2103 C  CZ  . ARG A 245 ? 0.0119 0.1549 0.1794 -0.0279 0.0130  -0.0309 245 ARG A CZ  
2104 N  NH1 . ARG A 245 ? 0.0151 0.1351 0.1680 -0.0298 0.0250  -0.0359 245 ARG A NH1 
2105 N  NH2 . ARG A 245 ? 0.0072 0.1583 0.2072 -0.0087 -0.0073 -0.0292 245 ARG A NH2 
2106 N  N   . PRO A 246 ? 0.0361 0.1115 0.1804 -0.0559 0.0259  -0.0496 246 PRO A N   
2107 C  CA  . PRO A 246 ? 0.0270 0.1084 0.1664 -0.0340 -0.0222 -0.0424 246 PRO A CA  
2108 C  C   . PRO A 246 ? 0.0335 0.1819 0.1518 -0.0601 -0.0121 -0.0502 246 PRO A C   
2109 O  O   . PRO A 246 ? 0.0225 0.1770 0.1766 -0.0522 0.0021  -0.0241 246 PRO A O   
2110 C  CB  . PRO A 246 ? 0.0613 0.1200 0.2054 -0.0776 0.0063  -0.0358 246 PRO A CB  
2111 C  CG  . PRO A 246 ? 0.1098 0.2480 0.3015 -0.1336 0.0391  -0.1679 246 PRO A CG  
2112 C  CD  . PRO A 246 ? 0.0831 0.2296 0.2178 -0.1307 0.0546  -0.0838 246 PRO A CD  
2113 N  N   . ALA A 247 ? 0.0385 0.1474 0.1574 -0.0611 -0.0065 -0.0483 247 ALA A N   
2114 C  CA  . ALA A 247 ? 0.0217 0.1085 0.1522 -0.0337 -0.0069 -0.0478 247 ALA A CA  
2115 C  C   . ALA A 247 ? 0.0259 0.1248 0.1339 -0.0453 0.0000  -0.0409 247 ALA A C   
2116 O  O   . ALA A 247 ? 0.0485 0.1347 0.1705 -0.0641 -0.0192 -0.0395 247 ALA A O   
2117 C  CB  . ALA A 247 ? 0.0419 0.1301 0.1694 -0.0305 0.0271  -0.0441 247 ALA A CB  
2118 N  N   . GLN A 248 ? 0.0257 0.1243 0.1522 -0.0427 -0.0113 -0.0328 248 GLN A N   
2119 C  CA  . GLN A 248 ? 0.0185 0.1406 0.1764 -0.0394 -0.0004 -0.0310 248 GLN A CA  
2120 C  C   . GLN A 248 ? 0.0401 0.1479 0.1789 -0.0576 -0.0294 -0.0294 248 GLN A C   
2121 O  O   . GLN A 248 ? 0.0351 0.1429 0.1608 -0.0568 -0.0008 -0.0458 248 GLN A O   
2122 C  CB  . GLN A 248 ? 0.0409 0.1371 0.1856 -0.0646 -0.0049 -0.0330 248 GLN A CB  
2123 C  CG  . GLN A 248 ? 0.0410 0.1270 0.1754 -0.0545 -0.0155 -0.0374 248 GLN A CG  
2124 C  CD  . GLN A 248 ? 0.0262 0.1810 0.1899 -0.0493 -0.0202 -0.0415 248 GLN A CD  
2125 O  OE1 . GLN A 248 ? 0.0239 0.1940 0.2087 -0.0386 -0.0026 -0.0132 248 GLN A OE1 
2126 N  NE2 . GLN A 248 ? 0.0268 0.1672 0.1796 -0.0168 -0.0070 -0.0376 248 GLN A NE2 
2127 N  N   . PRO A 249 ? 0.0296 0.2007 0.1812 -0.0570 -0.0242 -0.0311 249 PRO A N   
2128 C  CA  . PRO A 249 ? 0.0432 0.2112 0.1877 -0.0814 -0.0098 -0.0453 249 PRO A CA  
2129 C  C   . PRO A 249 ? 0.0387 0.1277 0.1779 -0.0583 -0.0067 -0.0401 249 PRO A C   
2130 O  O   . PRO A 249 ? 0.0597 0.1376 0.1629 -0.0707 -0.0161 -0.0537 249 PRO A O   
2131 C  CB  . PRO A 249 ? 0.1093 0.2780 0.2523 -0.1478 -0.0825 0.0150  249 PRO A CB  
2132 C  CG  . PRO A 249 ? 0.1105 0.3042 0.1860 -0.1051 -0.0762 0.0029  249 PRO A CG  
2133 C  CD  . PRO A 249 ? 0.0437 0.3050 0.2539 -0.0835 -0.0561 -0.0094 249 PRO A CD  
2134 N  N   . LEU A 250 ? 0.0626 0.1785 0.1418 -0.0898 -0.0020 -0.0590 250 LEU A N   
2135 C  CA  . LEU A 250 ? 0.0529 0.1360 0.1743 -0.0661 0.0120  -0.0458 250 LEU A CA  
2136 C  C   . LEU A 250 ? 0.1066 0.1412 0.1584 -0.0844 -0.0399 -0.0595 250 LEU A C   
2137 O  O   . LEU A 250 ? 0.0624 0.1388 0.1753 -0.0719 -0.0326 -0.0356 250 LEU A O   
2138 C  CB  . LEU A 250 ? 0.0209 0.1828 0.2034 -0.0430 -0.0001 -0.0651 250 LEU A CB  
2139 C  CG  . LEU A 250 ? 0.0594 0.2103 0.1872 -0.0593 0.0170  -0.0354 250 LEU A CG  
2140 C  CD1 . LEU A 250 ? 0.0554 0.2396 0.1952 -0.0519 -0.0116 -0.0133 250 LEU A CD1 
2141 C  CD2 . LEU A 250 ? 0.1577 0.2606 0.2625 -0.0111 0.0653  -0.0508 250 LEU A CD2 
2142 N  N   . LYS A 251 ? 0.0811 0.1893 0.1687 -0.0907 -0.0368 -0.0502 251 LYS A N   
2143 C  CA  . LYS A 251 ? 0.1831 0.2030 0.1462 -0.0908 -0.0345 -0.0356 251 LYS A CA  
2144 C  C   . LYS A 251 ? 0.0791 0.2124 0.2044 -0.0137 -0.0328 0.0054  251 LYS A C   
2145 O  O   . LYS A 251 ? 0.1288 0.2512 0.2569 -0.0154 -0.0025 -0.0313 251 LYS A O   
2146 C  CB  . LYS A 251 ? 0.1445 0.1976 0.1960 -0.0894 -0.0644 -0.0199 251 LYS A CB  
2147 C  CG  . LYS A 251 ? 0.1628 0.2610 0.3310 -0.0469 0.0135  0.0581  251 LYS A CG  
2148 C  CD  . LYS A 251 ? 0.2091 0.2981 0.3837 0.0089  -0.0325 0.0482  251 LYS A CD  
2149 C  CE  . LYS A 251 ? 0.2909 0.3139 0.4947 -0.0263 0.0825  -0.0131 251 LYS A CE  
2150 N  NZ  . LYS A 251 ? 0.2192 0.3415 0.4387 -0.0521 -0.1452 -0.1764 251 LYS A NZ  
2151 N  N   . ASN A 252 ? 0.1021 0.2214 0.1667 -0.0785 -0.0429 -0.0143 252 ASN A N   
2152 C  CA  . ASN A 252 ? 0.1678 0.3486 0.2064 -0.1010 -0.0129 0.0076  252 ASN A CA  
2153 C  C   . ASN A 252 ? 0.1787 0.3340 0.3459 -0.0989 -0.0815 0.0544  252 ASN A C   
2154 O  O   . ASN A 252 ? 0.1500 0.3209 0.4011 -0.1252 -0.0728 0.0027  252 ASN A O   
2155 C  CB  . ASN A 252 ? 0.1360 0.4186 0.3204 -0.0769 0.0033  0.0457  252 ASN A CB  
2156 C  CG  . ASN A 252 ? 0.4297 0.4279 0.3680 -0.1630 0.0864  0.0609  252 ASN A CG  
2157 O  OD1 . ASN A 252 ? 0.6443 0.6303 0.4839 0.0227  0.2395  0.0414  252 ASN A OD1 
2158 N  ND2 . ASN A 252 ? 0.2175 0.4048 0.5312 -0.0976 -0.1229 -0.0263 252 ASN A ND2 
2159 N  N   . ARG A 253 ? 0.0554 0.2667 0.1721 -0.0727 -0.0184 -0.0504 253 ARG A N   
2160 C  CA  . ARG A 253 ? 0.0444 0.1885 0.1497 -0.0746 0.0013  -0.0221 253 ARG A CA  
2161 C  C   . ARG A 253 ? 0.0795 0.1703 0.1685 -0.0736 0.0059  -0.0266 253 ARG A C   
2162 O  O   . ARG A 253 ? 0.1098 0.1793 0.2731 -0.0957 0.0412  -0.0582 253 ARG A O   
2163 C  CB  . ARG A 253 ? 0.0306 0.1777 0.1406 -0.0560 0.0046  -0.0217 253 ARG A CB  
2164 C  CG  . ARG A 253 ? 0.1134 0.1295 0.1507 -0.0690 -0.0013 -0.0177 253 ARG A CG  
2165 C  CD  . ARG A 253 ? 0.0649 0.1640 0.1603 -0.0859 -0.0291 -0.0232 253 ARG A CD  
2166 N  NE  . ARG A 253 ? 0.0644 0.1281 0.1530 -0.0724 -0.0194 -0.0423 253 ARG A NE  
2167 C  CZ  . ARG A 253 ? 0.0447 0.1354 0.1334 -0.0633 -0.0049 -0.0472 253 ARG A CZ  
2168 N  NH1 . ARG A 253 ? 0.0294 0.1249 0.1493 -0.0414 -0.0127 -0.0548 253 ARG A NH1 
2169 N  NH2 . ARG A 253 ? 0.0432 0.1342 0.1552 -0.0610 -0.0165 -0.0345 253 ARG A NH2 
2170 N  N   . GLN A 254 ? 0.0595 0.2156 0.1463 -0.0632 0.0117  -0.0073 254 GLN A N   
2171 C  CA  . GLN A 254 ? 0.0471 0.2655 0.1958 -0.0762 0.0183  -0.0237 254 GLN A CA  
2172 C  C   . GLN A 254 ? 0.1170 0.1516 0.1476 -0.0487 0.0106  -0.0260 254 GLN A C   
2173 O  O   . GLN A 254 ? 0.1542 0.1615 0.2579 -0.0262 -0.0262 -0.0651 254 GLN A O   
2174 C  CB  . GLN A 254 ? 0.1601 0.4051 0.2321 -0.0675 0.0579  0.0384  254 GLN A CB  
2175 C  CG  . GLN A 254 ? 0.3332 0.6218 0.2461 -0.1436 0.0229  0.0875  254 GLN A CG  
2176 C  CD  . GLN A 254 ? 0.1438 1.2151 0.4754 -0.3229 0.0837  -0.0675 254 GLN A CD  
2177 O  OE1 . GLN A 254 ? 0.0884 0.8438 1.0855 -0.2126 0.1163  -0.3665 254 GLN A OE1 
2178 N  NE2 . GLN A 254 ? 0.4459 0.8817 0.5176 -0.0864 -0.0113 -0.1574 254 GLN A NE2 
2179 N  N   . ILE A 255 ? 0.0937 0.1283 0.1370 -0.0635 -0.0008 -0.0399 255 ILE A N   
2180 C  CA  . ILE A 255 ? 0.0542 0.1509 0.1286 -0.0385 0.0108  -0.0537 255 ILE A CA  
2181 C  C   . ILE A 255 ? 0.0721 0.1458 0.1531 -0.0545 0.0398  -0.0542 255 ILE A C   
2182 O  O   . ILE A 255 ? 0.0748 0.1897 0.1746 -0.0687 0.0562  -0.0829 255 ILE A O   
2183 C  CB  . ILE A 255 ? 0.0588 0.1485 0.1421 -0.0495 0.0242  -0.0368 255 ILE A CB  
2184 C  CG1 . ILE A 255 ? 0.0489 0.1512 0.1824 -0.0634 0.0168  -0.0348 255 ILE A CG1 
2185 C  CG2 . ILE A 255 ? 0.0595 0.1646 0.1628 -0.0538 0.0072  -0.0432 255 ILE A CG2 
2186 C  CD1 . ILE A 255 ? 0.0827 0.1618 0.1576 -0.0309 0.0523  -0.0239 255 ILE A CD1 
2187 N  N   . LYS A 256 ? 0.0340 0.1512 0.1425 -0.0370 0.0324  -0.0444 256 LYS A N   
2188 C  CA  . LYS A 256 ? 0.0294 0.1418 0.1629 -0.0369 0.0300  -0.0491 256 LYS A CA  
2189 C  C   . LYS A 256 ? 0.0633 0.1407 0.1451 -0.0270 0.0346  -0.0447 256 LYS A C   
2190 O  O   . LYS A 256 ? 0.1060 0.1991 0.1415 -0.0063 0.0330  -0.0407 256 LYS A O   
2191 C  CB  . LYS A 256 ? 0.0784 0.1586 0.2055 -0.0403 0.0555  -0.0368 256 LYS A CB  
2192 C  CG  . LYS A 256 ? 0.1363 0.2183 0.2952 -0.0019 0.0364  -0.0100 256 LYS A CG  
2193 C  CD  . LYS A 256 ? 0.2504 0.2466 0.3574 -0.0842 0.0133  -0.0005 256 LYS A CD  
2194 C  CE  . LYS A 256 ? 0.2545 0.3871 0.4568 0.1111  0.1166  0.0559  256 LYS A CE  
2195 N  NZ  . LYS A 256 ? 0.3815 0.3763 0.7875 0.0735  0.1900  -0.0615 256 LYS A NZ  
2196 N  N   . ALA A 257 ? 0.0623 0.1601 0.1565 -0.0138 0.0550  -0.0340 257 ALA A N   
2197 C  CA  . ALA A 257 ? 0.0166 0.1849 0.2168 -0.0276 0.0428  -0.0579 257 ALA A CA  
2198 C  C   . ALA A 257 ? 0.0220 0.1859 0.1972 -0.0279 0.0485  -0.0365 257 ALA A C   
2199 O  O   . ALA A 257 ? 0.0776 0.2017 0.1795 -0.0494 0.0554  -0.0411 257 ALA A O   
2200 C  CB  . ALA A 257 ? 0.0437 0.1718 0.2237 -0.0300 0.0465  -0.0444 257 ALA A CB  
2201 N  N   . SER A 258 ? 0.0312 0.1524 0.1837 -0.0301 0.0499  -0.0395 258 SER A N   
2202 C  CA  . SER A 258 ? 0.0281 0.1804 0.2172 -0.0354 0.0443  -0.0420 258 SER A CA  
2203 C  C   . SER A 258 ? 0.0272 0.2385 0.1918 -0.0105 0.0514  -0.0245 258 SER A C   
2204 O  O   . SER A 258 ? 0.0386 0.3621 0.2480 -0.0434 0.0851  -0.0431 258 SER A O   
2205 C  CB  . SER A 258 ? 0.0280 0.1702 0.2170 -0.0532 0.0274  -0.0401 258 SER A CB  
2206 O  OG  . SER A 258 ? 0.0204 0.2163 0.1922 -0.0451 0.0323  -0.0358 258 SER A OG  
2207 N  N   . PHE A 259 ? 0.0455 0.2464 0.2854 -0.0252 0.1034  -0.0308 259 PHE A N   
2208 C  CA  . PHE A 259 ? 0.0936 0.2584 0.2713 0.0270  0.0702  -0.0386 259 PHE A CA  
2209 C  C   . PHE A 259 ? 0.1372 0.3080 0.3085 -0.0182 0.1173  -0.0580 259 PHE A C   
2210 O  O   . PHE A 259 ? 0.1455 0.2967 0.2966 0.0475  0.0632  -0.1024 259 PHE A O   
2211 C  CB  . PHE A 259 ? 0.0919 0.2606 0.3030 0.0110  0.0849  -0.0128 259 PHE A CB  
2212 C  CG  . PHE A 259 ? 0.0555 0.2071 0.3018 -0.0055 0.0260  -0.0680 259 PHE A CG  
2213 C  CD1 . PHE A 259 ? 0.0430 0.2559 0.2012 -0.0016 0.0270  -0.0143 259 PHE A CD1 
2214 C  CD2 . PHE A 259 ? 0.1934 0.2149 0.3818 -0.0105 0.1054  -0.0472 259 PHE A CD2 
2215 C  CE1 . PHE A 259 ? 0.0768 0.2007 0.2984 0.0003  0.0750  -0.0074 259 PHE A CE1 
2216 C  CE2 . PHE A 259 ? 0.1648 0.2360 0.3491 -0.0154 0.0254  -0.0262 259 PHE A CE2 
2217 C  CZ  . PHE A 259 ? 0.1016 0.2354 0.3837 -0.0576 0.0190  -0.0383 259 PHE A CZ  
2218 N  N   . LYS A 260 ? 0.2694 0.4102 0.3997 0.1107  0.1516  -0.1147 260 LYS A N   
2219 C  CA  . LYS A 260 ? 0.3863 0.5970 0.5939 -0.0032 0.1105  -0.3568 260 LYS A CA  
2220 C  C   . LYS A 260 ? 0.0901 0.8745 0.7425 0.0471  0.0253  -0.2966 260 LYS A C   
2221 O  O   . LYS A 260 ? 0.1040 1.2704 1.0839 -0.0567 0.2058  -0.1729 260 LYS A O   
2222 C  CB  . LYS A 260 ? 0.4784 0.5691 0.6481 0.0207  0.1719  -0.2819 260 LYS A CB  
2223 C  CG  . LYS A 260 ? 0.6843 0.6500 1.1878 0.0087  -0.0954 -0.2034 260 LYS A CG  
2224 C  CD  . LYS A 260 ? 1.0285 0.5930 1.0877 -0.0682 -0.0566 -0.2842 260 LYS A CD  
2225 C  CE  . LYS A 260 ? 1.0028 0.6014 1.0171 -0.3693 0.4769  -0.0429 260 LYS A CE  
2226 N  NZ  . LYS A 260 ? 0.7080 0.7835 0.9719 -0.2350 -0.0671 -0.1116 260 LYS A NZ  
2227 O  OXT . LYS A 260 ? 0.4983 0.9815 0.8724 -0.0504 -0.2167 -0.3561 260 LYS A OXT 
2228 C  CA  . HIS B 4   ? 1.3572 2.4159 0.9397 -1.4759 0.7864  -0.2435 4   HIS B CA  
2229 C  C   . HIS B 4   ? 0.2625 0.4913 0.4245 -0.2037 0.2095  0.1154  4   HIS B C   
2230 O  O   . HIS B 4   ? 0.4074 0.5136 0.4060 -0.0260 0.2160  -0.0568 4   HIS B O   
2231 C  CB  . HIS B 4   ? 0.6608 1.7441 0.7802 -0.3653 0.3436  0.4668  4   HIS B CB  
2232 C  CG  . HIS B 4   ? 0.5122 1.7035 0.8599 -0.4846 0.4081  0.1964  4   HIS B CG  
2233 N  ND1 . HIS B 4   ? 1.2505 1.7055 0.7074 -0.5475 -0.1037 0.1109  4   HIS B ND1 
2234 C  CD2 . HIS B 4   ? 1.2977 1.9495 0.9080 -0.4460 -0.0555 0.2346  4   HIS B CD2 
2235 C  CE1 . HIS B 4   ? 1.5829 2.1178 0.4083 -0.3955 -0.1810 0.2269  4   HIS B CE1 
2236 N  NE2 . HIS B 4   ? 1.1072 2.0488 0.9542 -0.4256 -0.4321 0.1664  4   HIS B NE2 
2237 N  N   . TRP B 5   ? 0.2293 0.3237 0.4590 -0.0543 0.1428  -0.0100 5   TRP B N   
2238 C  CA  . TRP B 5   ? 0.1888 0.2676 0.4493 -0.1214 0.0706  -0.1058 5   TRP B CA  
2239 C  C   . TRP B 5   ? 0.1043 0.2526 0.3318 -0.0903 0.1483  -0.1349 5   TRP B C   
2240 O  O   . TRP B 5   ? 0.2186 0.2949 0.4206 -0.0671 0.1117  -0.0648 5   TRP B O   
2241 C  CB  . TRP B 5   ? 0.1131 0.2075 0.3956 -0.1289 0.0113  -0.0982 5   TRP B CB  
2242 C  CG  . TRP B 5   ? 0.0931 0.2292 0.2565 -0.0974 0.0826  -0.0537 5   TRP B CG  
2243 C  CD1 . TRP B 5   ? 0.1554 0.2169 0.3494 -0.1400 0.0621  -0.0558 5   TRP B CD1 
2244 C  CD2 . TRP B 5   ? 0.0702 0.2152 0.2610 -0.0619 0.0778  -0.0776 5   TRP B CD2 
2245 N  NE1 . TRP B 5   ? 0.1905 0.2603 0.2969 -0.0784 0.1177  -0.0351 5   TRP B NE1 
2246 C  CE2 . TRP B 5   ? 0.1787 0.2145 0.2235 -0.0414 0.0551  -0.0517 5   TRP B CE2 
2247 C  CE3 . TRP B 5   ? 0.0546 0.2311 0.2241 -0.0934 0.0695  -0.1078 5   TRP B CE3 
2248 C  CZ2 . TRP B 5   ? 0.1786 0.2886 0.2029 -0.0013 0.0055  -0.0663 5   TRP B CZ2 
2249 C  CZ3 . TRP B 5   ? 0.0457 0.2290 0.2362 -0.0715 0.0778  -0.1056 5   TRP B CZ3 
2250 C  CH2 . TRP B 5   ? 0.1527 0.2631 0.2303 0.0207  0.0655  -0.0963 5   TRP B CH2 
2251 N  N   . GLY B 6   ? 0.0629 0.2325 0.3726 -0.0814 0.1245  -0.0958 6   GLY B N   
2252 C  CA  . GLY B 6   ? 0.1447 0.1926 0.3216 -0.0983 0.1231  -0.1274 6   GLY B CA  
2253 C  C   . GLY B 6   ? 0.0611 0.2146 0.3489 -0.0504 0.1365  -0.1059 6   GLY B C   
2254 O  O   . GLY B 6   ? 0.0648 0.1914 0.3466 -0.0701 0.1112  -0.1056 6   GLY B O   
2255 N  N   . TYR B 7   ? 0.1271 0.1847 0.3570 -0.0588 0.1533  -0.0819 7   TYR B N   
2256 C  CA  . TYR B 7   ? 0.0951 0.1847 0.4170 -0.0577 0.1382  -0.0644 7   TYR B CA  
2257 C  C   . TYR B 7   ? 0.1435 0.2813 0.5844 -0.0166 0.2124  -0.1604 7   TYR B C   
2258 O  O   . TYR B 7   ? 0.3359 0.2742 0.7984 -0.1936 0.1551  0.0114  7   TYR B O   
2259 C  CB  . TYR B 7   ? 0.0942 0.1782 0.3345 -0.0703 0.1381  -0.1267 7   TYR B CB  
2260 C  CG  . TYR B 7   ? 0.0375 0.1479 0.2356 -0.0600 0.0211  -0.0905 7   TYR B CG  
2261 C  CD1 . TYR B 7   ? 0.0430 0.1822 0.2777 -0.0795 0.0760  -0.1455 7   TYR B CD1 
2262 C  CD2 . TYR B 7   ? 0.0728 0.1645 0.2153 -0.0785 0.0621  -0.0716 7   TYR B CD2 
2263 C  CE1 . TYR B 7   ? 0.0380 0.1233 0.1931 -0.0605 0.0305  -0.0740 7   TYR B CE1 
2264 C  CE2 . TYR B 7   ? 0.0523 0.1726 0.1685 -0.0834 0.0447  -0.0798 7   TYR B CE2 
2265 C  CZ  . TYR B 7   ? 0.0430 0.1430 0.1703 -0.0636 0.0449  -0.0638 7   TYR B CZ  
2266 O  OH  . TYR B 7   ? 0.0640 0.1301 0.1635 -0.0477 0.0315  -0.0457 7   TYR B OH  
2267 N  N   . GLY B 8   ? 0.1251 0.3106 0.6797 -0.0819 0.1922  -0.1472 8   GLY B N   
2268 C  CA  . GLY B 8   ? 0.2357 0.3563 0.7662 -0.1298 0.1483  -0.0988 8   GLY B CA  
2269 C  C   . GLY B 8   ? 0.3657 0.3111 0.7465 -0.0172 0.1137  -0.0627 8   GLY B C   
2270 O  O   . GLY B 8   ? 0.2703 0.2971 0.6682 -0.0960 0.1608  -0.1467 8   GLY B O   
2271 N  N   . LYS B 9   ? 0.3377 0.2124 0.8500 -0.1443 0.2497  0.0158  9   LYS B N   
2272 C  CA  . LYS B 9   ? 0.5511 0.4603 0.7368 -0.0854 0.0700  -0.1427 9   LYS B CA  
2273 C  C   . LYS B 9   ? 0.1936 0.3071 0.6607 0.1182  -0.1648 -0.1087 9   LYS B C   
2274 O  O   . LYS B 9   ? 0.3727 0.2404 0.6208 0.0009  0.0033  -0.0579 9   LYS B O   
2275 C  CB  . LYS B 9   ? 0.1952 0.7659 1.2408 0.1214  0.1307  -0.2126 9   LYS B CB  
2276 C  CG  . LYS B 9   ? 0.5236 0.5449 0.4861 -0.1506 0.1978  0.0139  9   LYS B CG  
2277 N  N   . HIS B 10  ? 0.2797 0.2441 0.8499 0.0719  0.2240  -0.0902 10  HIS B N   
2278 C  CA  . HIS B 10  ? 0.3114 0.6791 0.6097 -0.0006 0.3315  0.0121  10  HIS B CA  
2279 C  C   . HIS B 10  ? 0.9162 0.5685 0.7663 0.1367  0.1833  0.2121  10  HIS B C   
2280 O  O   . HIS B 10  ? 0.2650 0.3916 1.3294 0.3145  0.1298  0.1003  10  HIS B O   
2281 C  CB  . HIS B 10  ? 0.2183 0.2234 0.6260 -0.0203 0.3298  -0.0197 10  HIS B CB  
2282 C  CG  . HIS B 10  ? 0.3639 0.2218 0.6103 0.0328  0.1606  0.0177  10  HIS B CG  
2283 N  ND1 . HIS B 10  ? 0.3347 0.1708 0.5746 -0.0525 0.2256  -0.0787 10  HIS B ND1 
2284 C  CD2 . HIS B 10  ? 0.2643 0.2922 0.5696 -0.0171 0.1541  0.0198  10  HIS B CD2 
2285 C  CE1 . HIS B 10  ? 0.1970 0.1791 0.5490 -0.0436 0.0837  -0.1047 10  HIS B CE1 
2286 N  NE2 . HIS B 10  ? 0.1468 0.2330 0.3693 -0.0901 0.1122  -0.0182 10  HIS B NE2 
2287 N  N   . ASN B 11  ? 1.1799 0.5823 1.7292 -0.2901 0.7755  -0.4619 11  ASN B N   
2288 C  CA  . ASN B 11  ? 0.1113 0.7853 0.5278 -0.2244 0.1682  -0.0851 11  ASN B CA  
2289 C  C   . ASN B 11  ? 0.0726 0.1615 0.4809 -0.0368 0.1770  -0.0839 11  ASN B C   
2290 O  O   . ASN B 11  ? 0.0753 0.1969 0.3550 -0.0151 0.1374  -0.0595 11  ASN B O   
2291 C  CB  . ASN B 11  ? 0.2405 0.6653 0.6553 -0.0196 0.3560  -0.1111 11  ASN B CB  
2292 C  CG  . ASN B 11  ? 0.4355 0.2059 0.4449 0.0144  0.2920  0.0088  11  ASN B CG  
2293 O  OD1 . ASN B 11  ? 0.2002 0.2694 0.5032 -0.0876 0.2288  -0.1117 11  ASN B OD1 
2294 N  ND2 . ASN B 11  ? 0.1631 0.2386 0.4323 -0.0572 0.1700  -0.1448 11  ASN B ND2 
2295 N  N   . GLY B 12  ? 0.0863 0.1773 0.4331 -0.0622 0.1791  -0.0833 12  GLY B N   
2296 C  CA  . GLY B 12  ? 0.0585 0.2104 0.3184 -0.0310 0.1275  -0.0686 12  GLY B CA  
2297 C  C   . GLY B 12  ? 0.0687 0.1333 0.3614 -0.0709 0.1198  -0.0597 12  GLY B C   
2298 O  O   . GLY B 12  ? 0.0449 0.1878 0.5059 -0.0592 0.1129  -0.0503 12  GLY B O   
2299 N  N   . PRO B 13  ? 0.0628 0.1270 0.2983 -0.0706 0.1021  -0.0687 13  PRO B N   
2300 C  CA  . PRO B 13  ? 0.0534 0.1858 0.3021 -0.0585 0.1113  -0.0795 13  PRO B CA  
2301 C  C   . PRO B 13  ? 0.0385 0.1335 0.3437 -0.0605 0.0754  -0.0959 13  PRO B C   
2302 O  O   . PRO B 13  ? 0.0322 0.1754 0.2991 -0.0516 0.0309  -0.0965 13  PRO B O   
2303 C  CB  . PRO B 13  ? 0.0730 0.1401 0.2872 -0.0943 0.0883  -0.1192 13  PRO B CB  
2304 C  CG  . PRO B 13  ? 0.0682 0.1655 0.2662 -0.0951 0.0962  -0.1108 13  PRO B CG  
2305 C  CD  . PRO B 13  ? 0.0687 0.1549 0.2605 -0.0640 0.0922  -0.0833 13  PRO B CD  
2306 N  N   . GLU B 14  ? 0.0441 0.1370 0.3491 -0.0582 0.0638  -0.0845 14  GLU B N   
2307 C  CA  . GLU B 14  ? 0.0958 0.1690 0.4076 -0.0395 0.0100  -0.0361 14  GLU B CA  
2308 C  C   . GLU B 14  ? 0.0271 0.1595 0.4284 0.0148  0.0620  -0.0709 14  GLU B C   
2309 O  O   . GLU B 14  ? 0.0367 0.2269 0.4347 -0.0005 0.0179  -0.0391 14  GLU B O   
2310 C  CB  . GLU B 14  ? 0.2174 0.1614 0.5498 -0.0273 0.0268  0.0298  14  GLU B CB  
2311 C  CG  . GLU B 14  ? 0.2672 0.1823 0.4641 -0.0571 0.0917  -0.0506 14  GLU B CG  
2312 C  CD  . GLU B 14  ? 0.1107 0.5190 0.4961 -0.0870 0.0589  -0.0554 14  GLU B CD  
2313 O  OE1 . GLU B 14  ? 0.1231 0.6948 0.6888 -0.0704 0.0936  -0.0550 14  GLU B OE1 
2314 O  OE2 . GLU B 14  ? 0.5736 0.6072 0.5691 -0.1118 -0.0873 -0.1773 14  GLU B OE2 
2315 N  N   . HIS B 15  ? 0.0207 0.1624 0.4189 -0.0105 0.0515  -0.0524 15  HIS B N   
2316 C  CA  . HIS B 15  ? 0.0231 0.2680 0.4631 -0.0563 0.0567  -0.0588 15  HIS B CA  
2317 C  C   . HIS B 15  ? 0.0465 0.2886 0.5533 -0.0429 0.0691  -0.1213 15  HIS B C   
2318 O  O   . HIS B 15  ? 0.0570 0.2599 0.6100 -0.0827 0.1121  -0.1552 15  HIS B O   
2319 C  CB  . HIS B 15  ? 0.0097 0.2315 0.4071 -0.0100 0.0118  -0.0572 15  HIS B CB  
2320 C  CG  . HIS B 15  ? 0.0369 0.2138 0.4624 -0.0323 0.0995  -0.0068 15  HIS B CG  
2321 N  ND1 . HIS B 15  ? 0.0398 0.2569 0.4870 0.0111  0.1075  -0.0669 15  HIS B ND1 
2322 C  CD2 . HIS B 15  ? 0.0863 0.2216 0.4448 0.0109  0.1124  -0.0205 15  HIS B CD2 
2323 C  CE1 . HIS B 15  ? 0.1643 0.2145 0.4791 -0.0276 0.1033  -0.0494 15  HIS B CE1 
2324 N  NE2 . HIS B 15  ? 0.1086 0.2117 0.4255 0.0214  0.0976  -0.0482 15  HIS B NE2 
2325 N  N   . TRP B 16  ? 0.4474 0.9496 0.4873 -0.1402 -0.0767 -0.3467 16  TRP B N   
2326 C  CA  . TRP B 16  ? 0.4843 0.9856 0.9427 -0.6047 -0.3518 0.0645  16  TRP B CA  
2327 C  C   . TRP B 16  ? 0.0148 0.2520 0.3571 -0.0456 0.0423  -0.2379 16  TRP B C   
2328 O  O   . TRP B 16  ? 0.0165 0.1963 0.4033 -0.0301 -0.0283 -0.0970 16  TRP B O   
2329 C  CB  . TRP B 16  ? 0.1495 0.8056 0.4117 -0.2799 0.0024  -0.1107 16  TRP B CB  
2330 C  CG  . TRP B 16  ? 0.0440 0.1510 0.2480 -0.0617 0.0061  -0.1120 16  TRP B CG  
2331 C  CD1 . TRP B 16  ? 0.0467 0.1299 0.2447 -0.0681 0.0271  -0.0641 16  TRP B CD1 
2332 C  CD2 . TRP B 16  ? 0.0497 0.1476 0.2770 -0.0730 0.0799  -0.0872 16  TRP B CD2 
2333 N  NE1 . TRP B 16  ? 0.0486 0.1630 0.2537 -0.0747 0.0839  -0.1044 16  TRP B NE1 
2334 C  CE2 . TRP B 16  ? 0.0348 0.1560 0.2640 -0.0574 0.0695  -0.0859 16  TRP B CE2 
2335 C  CE3 . TRP B 16  ? 0.0208 0.1460 0.2433 -0.0424 0.0452  -0.0948 16  TRP B CE3 
2336 C  CZ2 . TRP B 16  ? 0.0424 0.1660 0.2187 -0.0741 0.0633  -0.1036 16  TRP B CZ2 
2337 C  CZ3 . TRP B 16  ? 0.0374 0.1866 0.2641 -0.0691 0.0667  -0.0941 16  TRP B CZ3 
2338 C  CH2 . TRP B 16  ? 0.0572 0.1488 0.2467 -0.0669 0.0942  -0.0635 16  TRP B CH2 
2339 N  N   . HIS B 17  ? 0.0288 0.2543 0.4204 -0.0741 0.0544  -0.1514 17  HIS B N   
2340 C  CA  . HIS B 17  ? 0.0219 0.1786 0.3981 -0.0483 0.0039  -0.1052 17  HIS B CA  
2341 C  C   . HIS B 17  ? 0.0107 0.2241 0.4000 -0.0307 0.0061  -0.0902 17  HIS B C   
2342 O  O   . HIS B 17  ? 0.0112 0.2685 0.5098 -0.0340 0.0010  -0.1176 17  HIS B O   
2343 C  CB  . HIS B 17  ? 0.0185 0.2377 0.4096 -0.0447 -0.0137 -0.1110 17  HIS B CB  
2344 C  CG  . HIS B 17  ? 0.0116 0.2128 0.3960 0.0047  -0.0436 -0.0359 17  HIS B CG  
2345 N  ND1 . HIS B 17  ? 0.0314 0.2203 0.4732 -0.0216 -0.0555 -0.0315 17  HIS B ND1 
2346 C  CD2 . HIS B 17  ? 0.0143 0.2102 0.3596 -0.0176 0.0420  -0.0403 17  HIS B CD2 
2347 C  CE1 . HIS B 17  ? 0.0684 0.2211 0.4740 -0.0160 0.0212  -0.0061 17  HIS B CE1 
2348 N  NE2 . HIS B 17  ? 0.0305 0.2235 0.4427 0.0172  0.0326  -0.0013 17  HIS B NE2 
2349 N  N   . LYS B 18  ? 0.0121 0.2343 0.4626 -0.0313 0.0347  -0.0670 18  LYS B N   
2350 C  CA  . LYS B 18  ? 0.0560 0.1762 0.4406 -0.0886 0.0664  -0.0563 18  LYS B CA  
2351 C  C   . LYS B 18  ? 0.0823 0.2515 0.5442 -0.1194 -0.0699 -0.0550 18  LYS B C   
2352 O  O   . LYS B 18  ? 0.0559 0.2793 0.8274 -0.1031 -0.1045 0.0308  18  LYS B O   
2353 C  CB  . LYS B 18  ? 0.0363 0.3224 0.5737 -0.0967 0.0341  -0.0591 18  LYS B CB  
2354 C  CG  . LYS B 18  ? 0.0395 0.2782 0.4857 -0.0784 0.0920  -0.0784 18  LYS B CG  
2355 C  CD  . LYS B 18  ? 0.0267 0.2680 0.7573 -0.0301 0.1215  -0.1018 18  LYS B CD  
2356 C  CE  . LYS B 18  ? 0.0599 0.3791 0.6445 -0.1121 0.1439  -0.1150 18  LYS B CE  
2357 N  NZ  . LYS B 18  ? 0.0136 0.2345 0.4354 -0.0233 0.0498  -0.0444 18  LYS B NZ  
2358 N  N   . ASP B 19  ? 0.0259 0.2475 0.4919 -0.0670 -0.0221 0.0041  19  ASP B N   
2359 C  CA  . ASP B 19  ? 0.0673 0.1927 0.5564 -0.1057 0.0405  -0.0299 19  ASP B CA  
2360 C  C   . ASP B 19  ? 0.1542 0.2800 0.4155 0.0446  0.0432  0.0280  19  ASP B C   
2361 O  O   . ASP B 19  ? 0.2376 0.2353 0.4629 0.0016  0.0318  -0.0178 19  ASP B O   
2362 C  CB  . ASP B 19  ? 0.0299 0.3889 0.4646 -0.0200 0.0591  -0.0368 19  ASP B CB  
2363 C  CG  . ASP B 19  ? 0.0955 0.5211 0.4413 -0.0768 0.0902  -0.1514 19  ASP B CG  
2364 O  OD1 . ASP B 19  ? 0.1600 0.7005 0.6481 -0.1935 0.0098  -0.1567 19  ASP B OD1 
2365 O  OD2 . ASP B 19  ? 0.3271 0.6207 0.5497 -0.0566 0.0555  -0.2222 19  ASP B OD2 
2366 N  N   . PHE B 20  ? 0.0262 0.2165 0.4411 -0.0594 0.0719  -0.1390 20  PHE B N   
2367 C  CA  . PHE B 20  ? 0.0123 0.2684 1.0566 -0.0296 -0.0135 -0.2754 20  PHE B CA  
2368 C  C   . PHE B 20  ? 0.2042 0.1480 1.0483 -0.1174 -0.0096 -0.2513 20  PHE B C   
2369 O  O   . PHE B 20  ? 0.0433 0.1234 0.4278 -0.0455 0.0173  -0.1057 20  PHE B O   
2370 C  CB  . PHE B 20  ? 0.0610 0.5477 0.5891 -0.0508 -0.1020 -0.3450 20  PHE B CB  
2371 C  CG  . PHE B 20  ? 0.0392 0.5718 0.8295 -0.1127 -0.0709 -0.1030 20  PHE B CG  
2372 C  CD1 . PHE B 20  ? 0.0952 0.5236 0.3490 -0.1208 -0.0107 0.0085  20  PHE B CD1 
2373 C  CD2 . PHE B 20  ? 0.1885 0.6088 0.5111 -0.2127 -0.1637 0.0033  20  PHE B CD2 
2374 C  CE1 . PHE B 20  ? 0.4414 0.4258 0.3917 -0.0739 0.0282  0.0640  20  PHE B CE1 
2375 C  CE2 . PHE B 20  ? 0.4209 0.4145 0.6212 0.0687  0.2048  0.1038  20  PHE B CE2 
2376 C  CZ  . PHE B 20  ? 0.0866 0.4251 0.4289 -0.0894 0.1355  0.0973  20  PHE B CZ  
2377 N  N   . PRO B 21  ? 0.1648 0.4374 0.7508 -0.0819 0.1967  -0.1583 21  PRO B N   
2378 C  CA  . PRO B 21  ? 0.1177 0.6858 0.7722 -0.0544 0.2159  -0.1429 21  PRO B CA  
2379 C  C   . PRO B 21  ? 0.0118 0.3562 0.4659 -0.0424 0.0299  -0.1564 21  PRO B C   
2380 O  O   . PRO B 21  ? 0.1789 0.3198 0.4218 0.0559  -0.0611 -0.0706 21  PRO B O   
2381 C  CB  . PRO B 21  ? 0.4727 0.4105 0.6077 0.0810  -0.0081 -0.1482 21  PRO B CB  
2382 C  CG  . PRO B 21  ? 0.5427 0.6452 0.6910 0.0837  0.0879  0.0433  21  PRO B CG  
2383 C  CD  . PRO B 21  ? 0.2234 0.3215 0.8581 -0.0898 0.2694  0.0473  21  PRO B CD  
2384 N  N   . ILE B 22  ? 0.0533 0.1545 0.2867 -0.0337 -0.0205 -0.1026 22  ILE B N   
2385 C  CA  . ILE B 22  ? 0.0414 0.1296 0.3211 -0.0476 -0.0089 -0.0643 22  ILE B CA  
2386 C  C   . ILE B 22  ? 0.0205 0.1566 0.2992 -0.0269 -0.0314 -0.0886 22  ILE B C   
2387 O  O   . ILE B 22  ? 0.0290 0.1909 0.3080 -0.0491 -0.0141 -0.1200 22  ILE B O   
2388 C  CB  . ILE B 22  ? 0.0233 0.1586 0.2510 -0.0208 -0.0392 -0.0910 22  ILE B CB  
2389 C  CG1 . ILE B 22  ? 0.0385 0.1502 0.2640 -0.0592 -0.0063 -0.0721 22  ILE B CG1 
2390 C  CG2 . ILE B 22  ? 0.0579 0.2130 0.3105 -0.0563 -0.0697 -0.0985 22  ILE B CG2 
2391 C  CD1 . ILE B 22  ? 0.0569 0.1922 0.3321 -0.0266 -0.0361 -0.0985 22  ILE B CD1 
2392 N  N   . ALA B 23  ? 0.0337 0.1177 0.3233 -0.0433 -0.0190 -0.0842 23  ALA B N   
2393 C  CA  . ALA B 23  ? 0.0367 0.1728 0.3778 -0.0512 -0.0165 -0.1426 23  ALA B CA  
2394 C  C   . ALA B 23  ? 0.0281 0.1969 0.3862 -0.0368 -0.0398 -0.1317 23  ALA B C   
2395 O  O   . ALA B 23  ? 0.0266 0.1564 0.2495 -0.0502 -0.0052 -0.0666 23  ALA B O   
2396 C  CB  . ALA B 23  ? 0.0294 0.2016 0.3286 -0.0550 -0.0120 -0.1129 23  ALA B CB  
2397 N  N   . LYS B 24  ? 0.0314 0.2154 0.3748 -0.0394 -0.0498 -0.1206 24  LYS B N   
2398 C  CA  . LYS B 24  ? 0.0233 0.2520 0.3360 -0.0580 -0.0008 -0.1213 24  LYS B CA  
2399 C  C   . LYS B 24  ? 0.0161 0.2606 0.2794 -0.0102 -0.0451 -0.0809 24  LYS B C   
2400 O  O   . LYS B 24  ? 0.0564 0.3248 0.3138 -0.0708 -0.0730 -0.0611 24  LYS B O   
2401 C  CB  . LYS B 24  ? 0.0176 0.1767 0.4192 -0.0399 -0.0158 -0.0495 24  LYS B CB  
2402 C  CG  . LYS B 24  ? 0.0524 0.2436 0.3600 -0.0020 0.0094  -0.0594 24  LYS B CG  
2403 C  CD  . LYS B 24  ? 0.0637 0.3568 0.3461 0.0528  0.0229  -0.0047 24  LYS B CD  
2404 C  CE  . LYS B 24  ? 0.0827 0.3781 0.5074 0.0356  0.0744  -0.0148 24  LYS B CE  
2405 N  NZ  . LYS B 24  ? 0.2634 0.3529 0.6654 -0.0283 0.1277  0.0768  24  LYS B NZ  
2406 N  N   . GLY B 25  ? 0.0144 0.2510 0.3192 -0.0240 -0.0298 -0.0983 25  GLY B N   
2407 C  CA  . GLY B 25  ? 0.0816 0.2191 0.2482 -0.0606 -0.0148 -0.0851 25  GLY B CA  
2408 C  C   . GLY B 25  ? 0.0766 0.1935 0.1994 -0.0515 -0.0651 -0.0854 25  GLY B C   
2409 O  O   . GLY B 25  ? 0.0238 0.2147 0.2498 -0.0256 -0.0453 -0.0798 25  GLY B O   
2410 N  N   . GLU B 26  ? 0.0554 0.3001 0.2703 -0.0611 -0.0430 -0.1683 26  GLU B N   
2411 C  CA  . GLU B 26  ? 0.0748 0.2196 0.2116 0.0096  -0.0581 -0.1139 26  GLU B CA  
2412 C  C   . GLU B 26  ? 0.0529 0.1782 0.1588 -0.0092 -0.0176 -0.0515 26  GLU B C   
2413 O  O   . GLU B 26  ? 0.1019 0.2448 0.1369 -0.0510 -0.0219 -0.0484 26  GLU B O   
2414 C  CB  . GLU B 26  ? 0.0960 0.3015 0.2620 -0.0303 -0.0842 -0.1777 26  GLU B CB  
2415 C  CG  . GLU B 26  ? 0.0922 0.3613 0.3048 -0.0458 -0.0972 -0.1070 26  GLU B CG  
2416 C  CD  . GLU B 26  ? 0.1684 0.4898 0.2540 -0.0117 -0.0980 -0.0532 26  GLU B CD  
2417 O  OE1 . GLU B 26  ? 0.2762 0.4996 0.3450 -0.1261 -0.1421 -0.0147 26  GLU B OE1 
2418 O  OE2 . GLU B 26  ? 0.1749 0.5676 0.5413 0.0705  -0.1274 -0.1034 26  GLU B OE2 
2419 N  N   . ARG B 27  ? 0.0274 0.1479 0.1533 -0.0349 -0.0187 -0.0729 27  ARG B N   
2420 C  CA  . ARG B 27  ? 0.0181 0.1640 0.1584 -0.0291 -0.0126 -0.0776 27  ARG B CA  
2421 C  C   . ARG B 27  ? 0.0414 0.1054 0.1522 -0.0416 -0.0158 -0.0642 27  ARG B C   
2422 O  O   . ARG B 27  ? 0.0168 0.1342 0.1459 -0.0273 -0.0117 -0.0535 27  ARG B O   
2423 C  CB  . ARG B 27  ? 0.0675 0.1481 0.1486 -0.0264 -0.0054 -0.0575 27  ARG B CB  
2424 C  CG  . ARG B 27  ? 0.0315 0.2012 0.2495 -0.0586 -0.0215 -0.0650 27  ARG B CG  
2425 C  CD  . ARG B 27  ? 0.0708 0.1274 0.2011 -0.0758 -0.0092 -0.0677 27  ARG B CD  
2426 N  NE  . ARG B 27  ? 0.0719 0.1377 0.1724 -0.0421 0.0046  -0.0794 27  ARG B NE  
2427 C  CZ  . ARG B 27  ? 0.0247 0.1958 0.1364 -0.0195 0.0255  -0.0603 27  ARG B CZ  
2428 N  NH1 . ARG B 27  ? 0.0624 0.2005 0.1543 -0.0211 0.0194  -0.0794 27  ARG B NH1 
2429 N  NH2 . ARG B 27  ? 0.0572 0.1745 0.1818 -0.0218 -0.0044 -0.0330 27  ARG B NH2 
2430 N  N   . GLN B 28  ? 0.0146 0.1457 0.1579 -0.0303 0.0028  -0.0758 28  GLN B N   
2431 C  CA  . GLN B 28  ? 0.0125 0.1337 0.1590 -0.0178 -0.0067 -0.0851 28  GLN B CA  
2432 C  C   . GLN B 28  ? 0.0137 0.1154 0.1365 -0.0266 0.0037  -0.0533 28  GLN B C   
2433 O  O   . GLN B 28  ? 0.0214 0.1409 0.1254 -0.0339 -0.0126 -0.0517 28  GLN B O   
2434 C  CB  . GLN B 28  ? 0.0108 0.1380 0.2351 -0.0217 -0.0030 -0.0609 28  GLN B CB  
2435 C  CG  . GLN B 28  ? 0.0277 0.1378 0.2369 -0.0410 -0.0026 -0.1049 28  GLN B CG  
2436 C  CD  . GLN B 28  ? 0.0196 0.1918 0.2242 -0.0477 0.0047  -0.0711 28  GLN B CD  
2437 O  OE1 . GLN B 28  ? 0.0247 0.1502 0.2124 -0.0471 0.0011  -0.0726 28  GLN B OE1 
2438 N  NE2 . GLN B 28  ? 0.0238 0.1615 0.2351 -0.0488 -0.0069 -0.0473 28  GLN B NE2 
2439 N  N   . SER B 29  ? 0.0125 0.1393 0.1447 -0.0212 -0.0017 -0.0843 29  SER B N   
2440 C  CA  . SER B 29  ? 0.0143 0.0919 0.1344 -0.0161 -0.0076 -0.0640 29  SER B CA  
2441 C  C   . SER B 29  ? 0.0315 0.1007 0.1261 -0.0461 0.0182  -0.0654 29  SER B C   
2442 O  O   . SER B 29  ? 0.0182 0.1121 0.1633 -0.0351 0.0183  -0.0697 29  SER B O   
2443 C  CB  . SER B 29  ? 0.0095 0.0928 0.1271 -0.0129 -0.0014 -0.0576 29  SER B CB  
2444 O  OG  . SER B 29  ? 0.0166 0.0992 0.1407 -0.0308 0.0186  -0.0640 29  SER B OG  
2445 N  N   . PRO B 30  ? 0.0172 0.0949 0.1424 -0.0303 0.0147  -0.0628 30  PRO B N   
2446 C  CA  . PRO B 30  ? 0.0238 0.1066 0.1321 -0.0417 0.0207  -0.0603 30  PRO B CA  
2447 C  C   . PRO B 30  ? 0.0116 0.1068 0.1231 -0.0231 0.0163  -0.0635 30  PRO B C   
2448 O  O   . PRO B 30  ? 0.0136 0.1251 0.1470 -0.0257 -0.0002 -0.0617 30  PRO B O   
2449 C  CB  . PRO B 30  ? 0.0132 0.0975 0.1152 -0.0247 0.0116  -0.0564 30  PRO B CB  
2450 C  CG  . PRO B 30  ? 0.0216 0.1163 0.1566 -0.0409 0.0226  -0.0661 30  PRO B CG  
2451 C  CD  . PRO B 30  ? 0.0289 0.1195 0.1555 -0.0491 0.0194  -0.0710 30  PRO B CD  
2452 N  N   . VAL B 31  ? 0.0189 0.0976 0.1203 -0.0332 0.0255  -0.0527 31  VAL B N   
2453 C  CA  . VAL B 31  ? 0.0113 0.1199 0.1346 -0.0227 0.0030  -0.0480 31  VAL B CA  
2454 C  C   . VAL B 31  ? 0.0149 0.1130 0.1154 -0.0278 -0.0004 -0.0404 31  VAL B C   
2455 O  O   . VAL B 31  ? 0.0146 0.1122 0.1348 -0.0260 -0.0049 -0.0384 31  VAL B O   
2456 C  CB  . VAL B 31  ? 0.0153 0.1420 0.1380 -0.0330 0.0050  -0.0607 31  VAL B CB  
2457 C  CG1 . VAL B 31  ? 0.0238 0.1292 0.1441 -0.0409 0.0050  -0.0706 31  VAL B CG1 
2458 C  CG2 . VAL B 31  ? 0.0113 0.1343 0.1525 -0.0227 0.0196  -0.0497 31  VAL B CG2 
2459 N  N   . ASP B 32  ? 0.0098 0.1188 0.1213 -0.0183 0.0007  -0.0456 32  ASP B N   
2460 C  CA  . ASP B 32  ? 0.0200 0.1186 0.1421 -0.0334 -0.0069 -0.0385 32  ASP B CA  
2461 C  C   . ASP B 32  ? 0.0331 0.1229 0.1226 -0.0451 -0.0030 -0.0374 32  ASP B C   
2462 O  O   . ASP B 32  ? 0.0590 0.1473 0.1398 -0.0307 -0.0055 -0.0586 32  ASP B O   
2463 C  CB  . ASP B 32  ? 0.0310 0.1235 0.1389 -0.0288 -0.0092 -0.0434 32  ASP B CB  
2464 C  CG  . ASP B 32  ? 0.0192 0.1518 0.1582 -0.0368 0.0118  -0.0379 32  ASP B CG  
2465 O  OD1 . ASP B 32  ? 0.0495 0.1159 0.1597 -0.0264 -0.0008 -0.0403 32  ASP B OD1 
2466 O  OD2 . ASP B 32  ? 0.1291 0.1584 0.1688 -0.0326 0.0075  -0.0266 32  ASP B OD2 
2467 N  N   . ILE B 33  ? 0.0194 0.1120 0.1320 -0.0219 0.0024  -0.0383 33  ILE B N   
2468 C  CA  . ILE B 33  ? 0.0342 0.1615 0.1270 -0.0276 0.0233  -0.0174 33  ILE B CA  
2469 C  C   . ILE B 33  ? 0.0545 0.1242 0.1400 -0.0256 0.0192  -0.0308 33  ILE B C   
2470 O  O   . ILE B 33  ? 0.0613 0.1421 0.1445 -0.0313 0.0222  -0.0314 33  ILE B O   
2471 C  CB  . ILE B 33  ? 0.0186 0.1430 0.1507 -0.0368 0.0262  -0.0364 33  ILE B CB  
2472 C  CG1 . ILE B 33  ? 0.0295 0.1527 0.1532 -0.0156 0.0417  -0.0159 33  ILE B CG1 
2473 C  CG2 . ILE B 33  ? 0.0195 0.1867 0.1706 -0.0047 0.0374  -0.0303 33  ILE B CG2 
2474 C  CD1 . ILE B 33  ? 0.0252 0.1736 0.1791 -0.0356 0.0266  -0.0081 33  ILE B CD1 
2475 N  N   A ASP B 34  ? 0.0507 0.1632 0.1317 -0.0498 0.0380  -0.0250 34  ASP B N   
2476 N  N   B ASP B 34  ? 0.1124 0.1629 0.1416 0.0002  0.0187  -0.0279 34  ASP B N   
2477 C  CA  A ASP B 34  ? 0.1273 0.1588 0.1314 -0.0148 0.0593  -0.0146 34  ASP B CA  
2478 C  CA  B ASP B 34  ? 0.1384 0.1745 0.1500 -0.0050 0.0468  -0.0182 34  ASP B CA  
2479 C  C   A ASP B 34  ? 0.1335 0.1684 0.1247 -0.0141 0.0659  -0.0166 34  ASP B C   
2480 C  C   B ASP B 34  ? 0.1385 0.1748 0.1550 -0.0131 0.0538  -0.0156 34  ASP B C   
2481 O  O   A ASP B 34  ? 0.2411 0.1840 0.1670 0.0027  0.0923  -0.0384 34  ASP B O   
2482 O  O   B ASP B 34  ? 0.2344 0.1815 0.1934 -0.0039 0.1008  -0.0255 34  ASP B O   
2483 C  CB  A ASP B 34  ? 0.2244 0.1624 0.1338 0.0168  0.0107  -0.0055 34  ASP B CB  
2484 C  CB  B ASP B 34  ? 0.2371 0.2250 0.1810 0.0436  -0.0161 -0.0055 34  ASP B CB  
2485 C  CG  A ASP B 34  ? 0.1617 0.1516 0.1592 -0.0337 -0.0017 -0.0155 34  ASP B CG  
2486 C  CG  B ASP B 34  ? 0.1923 0.2430 0.1997 0.0209  -0.0260 -0.0016 34  ASP B CG  
2487 O  OD1 A ASP B 34  ? 0.2136 0.2184 0.1845 0.0635  0.0037  0.0077  34  ASP B OD1 
2488 O  OD1 B ASP B 34  ? 0.1882 0.3280 0.1610 0.0416  -0.0073 0.0369  34  ASP B OD1 
2489 O  OD2 A ASP B 34  ? 0.1726 0.1383 0.1699 -0.0369 0.0089  -0.0156 34  ASP B OD2 
2490 O  OD2 B ASP B 34  ? 0.0987 0.3523 0.2741 -0.0285 0.0025  0.1015  34  ASP B OD2 
2491 N  N   . THR B 35  ? 0.1341 0.1569 0.1636 -0.0034 0.0583  -0.0084 35  THR B N   
2492 C  CA  . THR B 35  ? 0.1720 0.2258 0.1983 0.0665  0.1003  -0.0179 35  THR B CA  
2493 C  C   . THR B 35  ? 0.1539 0.2250 0.2127 0.0240  0.1254  -0.0013 35  THR B C   
2494 O  O   . THR B 35  ? 0.2785 0.2028 0.2495 0.0618  0.1650  -0.0200 35  THR B O   
2495 C  CB  . THR B 35  ? 0.1547 0.2499 0.2207 0.0310  0.0908  0.0162  35  THR B CB  
2496 O  OG1 . THR B 35  ? 0.1727 0.2567 0.2194 0.0212  0.0907  0.0212  35  THR B OG1 
2497 C  CG2 . THR B 35  ? 0.2134 0.2090 0.1900 -0.0183 0.0621  -0.0131 35  THR B CG2 
2498 N  N   A HIS B 36  ? 0.3097 0.2310 0.1972 0.0770  0.1456  0.0166  36  HIS B N   
2499 N  N   B HIS B 36  ? 0.3044 0.2367 0.2056 0.0684  0.1328  0.0278  36  HIS B N   
2500 C  CA  A HIS B 36  ? 0.3563 0.2022 0.1733 0.0542  0.1073  -0.0037 36  HIS B CA  
2501 C  CA  B HIS B 36  ? 0.3458 0.2512 0.2065 0.0329  0.1372  0.0200  36  HIS B CA  
2502 C  C   A HIS B 36  ? 0.3037 0.2093 0.1552 0.0533  0.1062  -0.0119 36  HIS B C   
2503 C  C   B HIS B 36  ? 0.3890 0.2524 0.1694 0.0569  0.1137  0.0271  36  HIS B C   
2504 O  O   A HIS B 36  ? 0.1007 0.2622 0.1474 0.0886  0.0190  -0.0303 36  HIS B O   
2505 O  O   B HIS B 36  ? 0.4438 0.3220 0.1804 0.0958  0.0806  0.0908  36  HIS B O   
2506 C  CB  A HIS B 36  ? 0.3180 0.1963 0.1613 0.0688  0.0958  -0.0201 36  HIS B CB  
2507 C  CB  B HIS B 36  ? 0.3160 0.2359 0.3153 -0.0429 0.0265  0.1106  36  HIS B CB  
2508 C  CG  A HIS B 36  ? 0.2978 0.1341 0.2013 0.0784  0.1101  -0.0252 36  HIS B CG  
2509 C  CG  B HIS B 36  ? 0.3134 0.2235 0.3999 0.0414  -0.0861 0.0651  36  HIS B CG  
2510 N  ND1 A HIS B 36  ? 0.2843 0.2083 0.1254 0.0430  0.0475  -0.0282 36  HIS B ND1 
2511 N  ND1 B HIS B 36  ? 0.3139 0.1445 0.3453 -0.1283 -0.1571 -0.0620 36  HIS B ND1 
2512 C  CD2 A HIS B 36  ? 0.4198 0.0833 0.1546 -0.0111 -0.0076 -0.0249 36  HIS B CD2 
2513 C  CD2 B HIS B 36  ? 0.3650 0.2568 0.5479 -0.0863 -0.1594 -0.0201 36  HIS B CD2 
2514 C  CE1 A HIS B 36  ? 0.4281 0.2132 0.1604 0.0575  -0.0146 -0.0469 36  HIS B CE1 
2515 C  CE1 B HIS B 36  ? 0.1124 0.2230 0.5633 -0.1479 -0.1288 0.1150  36  HIS B CE1 
2516 N  NE2 A HIS B 36  ? 0.3777 0.2066 0.2293 0.0217  0.0240  -0.0161 36  HIS B NE2 
2517 N  NE2 B HIS B 36  ? 0.3729 0.1978 0.4508 0.0611  0.0015  0.0322  36  HIS B NE2 
2518 N  N   . THR B 37  ? 0.2843 0.2329 0.1896 0.0462  0.0897  0.0071  37  THR B N   
2519 C  CA  . THR B 37  ? 0.3274 0.2464 0.1875 0.0385  0.0337  0.0070  37  THR B CA  
2520 C  C   . THR B 37  ? 0.2918 0.2718 0.1381 0.0903  0.0475  -0.0133 37  THR B C   
2521 O  O   . THR B 37  ? 0.4959 0.3203 0.1601 0.0803  0.0076  -0.0582 37  THR B O   
2522 C  CB  . THR B 37  ? 0.3102 0.2886 0.2740 0.0983  -0.1051 -0.0457 37  THR B CB  
2523 O  OG1 . THR B 37  ? 0.3376 0.2937 0.3791 0.0608  -0.0153 0.0002  37  THR B OG1 
2524 C  CG2 . THR B 37  ? 0.5355 0.2828 0.2146 0.0240  -0.0487 -0.0590 37  THR B CG2 
2525 N  N   . ALA B 38  ? 0.1930 0.2429 0.1509 0.0472  0.0554  -0.0040 38  ALA B N   
2526 C  CA  . ALA B 38  ? 0.1558 0.2360 0.1602 0.0507  0.0551  -0.0118 38  ALA B CA  
2527 C  C   . ALA B 38  ? 0.2548 0.2865 0.3143 0.0793  0.1662  -0.0017 38  ALA B C   
2528 O  O   . ALA B 38  ? 0.3666 0.2784 0.4005 0.0748  0.2520  0.0186  38  ALA B O   
2529 C  CB  . ALA B 38  ? 0.1732 0.2373 0.1705 0.0288  0.0355  -0.0060 38  ALA B CB  
2530 N  N   A LYS B 39  ? 0.2384 0.3313 0.2628 0.1736  0.0414  -0.0326 39  LYS B N   
2531 N  N   B LYS B 39  ? 0.3188 0.3325 0.2016 0.1254  0.0709  -0.0550 39  LYS B N   
2532 C  CA  A LYS B 39  ? 0.2349 0.3607 0.2320 0.1297  0.0381  -0.0457 39  LYS B CA  
2533 C  CA  B LYS B 39  ? 0.2192 0.3413 0.2470 0.1187  0.0422  -0.0480 39  LYS B CA  
2534 C  C   A LYS B 39  ? 0.0544 0.3202 0.2087 0.0002  -0.0158 -0.1040 39  LYS B C   
2535 C  C   B LYS B 39  ? 0.0644 0.3106 0.2135 -0.0161 -0.0248 -0.1072 39  LYS B C   
2536 O  O   A LYS B 39  ? 0.1233 0.2896 0.2037 0.0273  0.0691  -0.0717 39  LYS B O   
2537 O  O   B LYS B 39  ? 0.1294 0.2847 0.2070 0.0025  0.0679  -0.0697 39  LYS B O   
2538 C  CB  A LYS B 39  ? 0.1394 0.3509 0.2675 0.0050  0.0435  -0.0730 39  LYS B CB  
2539 C  CB  B LYS B 39  ? 0.3148 0.2074 0.4063 -0.0142 -0.0273 -0.0810 39  LYS B CB  
2540 C  CG  A LYS B 39  ? 0.1333 0.3553 0.1936 -0.0319 0.0092  -0.0728 39  LYS B CG  
2541 C  CG  B LYS B 39  ? 0.2710 0.1885 0.3655 -0.1382 -0.1163 -0.0341 39  LYS B CG  
2542 C  CD  A LYS B 39  ? 0.3339 0.3753 0.3869 -0.0002 0.0436  -0.0216 39  LYS B CD  
2543 C  CD  B LYS B 39  ? 0.2466 0.3516 0.3953 0.0281  -0.0946 -0.0536 39  LYS B CD  
2544 C  CE  A LYS B 39  ? 0.2540 0.4295 0.2681 0.0442  -0.0008 0.1534  39  LYS B CE  
2545 C  CE  B LYS B 39  ? 0.2938 0.2455 0.3622 0.0151  -0.2098 -0.0391 39  LYS B CE  
2546 N  NZ  A LYS B 39  ? 0.1470 0.5562 0.3838 0.0473  0.0765  0.1791  39  LYS B NZ  
2547 N  NZ  B LYS B 39  ? 0.4684 0.3644 0.4622 -0.0375 -0.0706 -0.0548 39  LYS B NZ  
2548 N  N   . TYR B 40  ? 0.0915 0.3528 0.2473 -0.0037 0.0489  -0.0611 40  TYR B N   
2549 C  CA  . TYR B 40  ? 0.0809 0.2436 0.2392 -0.0229 0.0328  -0.0641 40  TYR B CA  
2550 C  C   . TYR B 40  ? 0.1019 0.2560 0.1914 0.0026  0.0145  -0.0435 40  TYR B C   
2551 O  O   . TYR B 40  ? 0.1164 0.2963 0.1919 0.0084  0.0556  -0.0525 40  TYR B O   
2552 C  CB  . TYR B 40  ? 0.1629 0.4250 0.2458 -0.1159 0.0629  -0.0151 40  TYR B CB  
2553 C  CG  . TYR B 40  ? 0.1564 0.4646 0.2311 -0.1232 0.0961  -0.0829 40  TYR B CG  
2554 C  CD1 . TYR B 40  ? 0.2279 0.2701 0.2821 -0.1127 0.0538  -0.0560 40  TYR B CD1 
2555 C  CD2 . TYR B 40  ? 0.1914 0.5709 0.3080 -0.0380 0.1581  -0.0480 40  TYR B CD2 
2556 C  CE1 . TYR B 40  ? 0.1454 0.4890 0.2586 -0.1163 0.0532  -0.0302 40  TYR B CE1 
2557 C  CE2 . TYR B 40  ? 0.2005 0.6108 0.2798 -0.0073 0.0977  0.0256  40  TYR B CE2 
2558 C  CZ  . TYR B 40  ? 0.1077 0.6235 0.2667 -0.0638 0.0425  -0.0083 40  TYR B CZ  
2559 O  OH  . TYR B 40  ? 0.1637 0.6516 0.3768 0.0134  0.0790  -0.1324 40  TYR B OH  
2560 N  N   . ASP B 41  ? 0.0879 0.2210 0.1759 -0.0128 0.0245  -0.0558 41  ASP B N   
2561 C  CA  . ASP B 41  ? 0.0818 0.2213 0.2223 -0.0188 0.0142  -0.0594 41  ASP B CA  
2562 C  C   . ASP B 41  ? 0.0402 0.2694 0.2375 -0.0361 0.0614  -0.0475 41  ASP B C   
2563 O  O   . ASP B 41  ? 0.0870 0.3459 0.2367 0.0039  0.0244  -0.0685 41  ASP B O   
2564 C  CB  . ASP B 41  ? 0.1114 0.1923 0.3128 -0.0445 -0.0174 -0.0331 41  ASP B CB  
2565 C  CG  . ASP B 41  ? 0.1363 0.2503 0.3978 -0.0446 -0.0671 -0.1356 41  ASP B CG  
2566 O  OD1 . ASP B 41  ? 0.2320 0.3234 0.3159 0.0113  -0.0528 -0.1492 41  ASP B OD1 
2567 O  OD2 . ASP B 41  ? 0.2122 0.2441 0.4512 -0.0766 -0.1342 -0.0751 41  ASP B OD2 
2568 N  N   . PRO B 42  ? 0.1311 0.4065 0.2287 0.0314  0.0907  -0.0631 42  PRO B N   
2569 C  CA  . PRO B 42  ? 0.1447 0.4557 0.3304 0.0692  0.1062  -0.0277 42  PRO B CA  
2570 C  C   . PRO B 42  ? 0.1678 0.4201 0.3307 0.0432  0.0643  -0.0464 42  PRO B C   
2571 O  O   . PRO B 42  ? 0.1868 0.4806 0.4387 0.0527  0.0301  -0.0863 42  PRO B O   
2572 C  CB  . PRO B 42  ? 0.2027 0.4769 0.3134 0.0081  0.1304  -0.0759 42  PRO B CB  
2573 C  CG  . PRO B 42  ? 0.2224 0.6339 0.2770 0.1878  0.0982  -0.0441 42  PRO B CG  
2574 C  CD  . PRO B 42  ? 0.1348 0.5138 0.2546 0.0725  0.0955  -0.0280 42  PRO B CD  
2575 N  N   . SER B 43  ? 0.1672 0.3546 0.2949 0.0756  0.0541  -0.1167 43  SER B N   
2576 C  CA  . SER B 43  ? 0.3489 0.3464 0.3264 0.0589  0.0102  -0.0911 43  SER B CA  
2577 C  C   . SER B 43  ? 0.1019 0.3934 0.3383 0.0739  -0.0051 -0.0701 43  SER B C   
2578 O  O   . SER B 43  ? 0.4114 0.3630 0.3912 0.0738  -0.0530 -0.0368 43  SER B O   
2579 C  CB  . SER B 43  ? 0.1238 0.6080 0.5449 -0.1427 0.0226  0.0599  43  SER B CB  
2580 O  OG  . SER B 43  ? 0.2776 0.3610 0.3708 -0.0356 -0.0754 -0.1480 43  SER B OG  
2581 N  N   . LEU B 44  ? 0.2493 0.4365 0.2896 0.1483  0.0344  -0.0535 44  LEU B N   
2582 C  CA  . LEU B 44  ? 0.1164 0.4867 0.2810 0.0379  0.0078  -0.0506 44  LEU B CA  
2583 C  C   . LEU B 44  ? 0.1301 0.5134 0.4106 -0.1115 -0.0309 0.0903  44  LEU B C   
2584 O  O   . LEU B 44  ? 0.1417 0.4896 0.4062 -0.0884 0.0577  0.0259  44  LEU B O   
2585 C  CB  . LEU B 44  ? 0.0842 0.3185 0.3070 -0.0960 0.0150  -0.0525 44  LEU B CB  
2586 C  CG  . LEU B 44  ? 0.0895 0.3208 0.3624 -0.1615 0.0691  -0.1190 44  LEU B CG  
2587 C  CD1 . LEU B 44  ? 0.0852 0.2855 0.2753 -0.0630 0.0324  -0.0300 44  LEU B CD1 
2588 C  CD2 . LEU B 44  ? 0.0869 0.2506 0.2522 -0.0971 -0.0129 -0.0497 44  LEU B CD2 
2589 N  N   . LYS B 45  ? 0.0927 0.3757 0.3406 -0.0321 0.0297  -0.0301 45  LYS B N   
2590 C  CA  . LYS B 45  ? 0.1621 0.2945 0.4293 -0.0383 -0.0509 -0.0111 45  LYS B CA  
2591 C  C   . LYS B 45  ? 0.0996 0.4056 0.3768 0.0347  -0.0131 -0.0131 45  LYS B C   
2592 O  O   . LYS B 45  ? 0.0939 0.4963 0.3632 -0.0096 0.0211  -0.1443 45  LYS B O   
2593 C  CB  . LYS B 45  ? 0.1115 0.2449 0.4837 -0.0462 -0.0429 -0.0691 45  LYS B CB  
2594 C  CG  . LYS B 45  ? 0.1782 0.4066 0.3944 0.0179  -0.0401 -0.0631 45  LYS B CG  
2595 C  CD  . LYS B 45  ? 0.3474 0.4768 0.6113 0.0337  0.0558  0.1261  45  LYS B CD  
2596 C  CE  . LYS B 45  ? 0.3583 0.5778 0.8019 0.0543  0.0542  -0.1143 45  LYS B CE  
2597 N  N   . PRO B 46  ? 0.1066 0.4040 0.3393 -0.0817 0.0274  -0.0058 46  PRO B N   
2598 C  CA  . PRO B 46  ? 0.0750 0.6018 0.3951 -0.1917 0.0400  -0.0517 46  PRO B CA  
2599 C  C   . PRO B 46  ? 0.0396 0.3646 0.3164 0.0016  0.0894  0.0119  46  PRO B C   
2600 O  O   . PRO B 46  ? 0.0136 0.4230 0.3980 -0.0550 -0.0096 0.0402  46  PRO B O   
2601 C  CB  . PRO B 46  ? 0.0545 0.4955 0.4889 -0.1184 0.0925  0.0181  46  PRO B CB  
2602 C  CG  . PRO B 46  ? 0.1154 0.4359 0.4159 -0.0343 0.0621  -0.1928 46  PRO B CG  
2603 C  CD  . PRO B 46  ? 0.1342 0.2546 0.4253 -0.1024 0.0844  -0.1144 46  PRO B CD  
2604 N  N   . LEU B 47  ? 0.0144 0.4430 0.3383 -0.0511 0.0314  -0.0464 47  LEU B N   
2605 C  CA  . LEU B 47  ? 0.0517 0.2882 0.2901 -0.0813 0.0267  -0.0534 47  LEU B CA  
2606 C  C   . LEU B 47  ? 0.0348 0.2398 0.4376 -0.0794 0.0207  0.0121  47  LEU B C   
2607 O  O   . LEU B 47  ? 0.0610 0.2954 0.5389 -0.1244 -0.0428 0.0428  47  LEU B O   
2608 C  CB  . LEU B 47  ? 0.2383 0.3794 0.4533 0.0565  0.0147  -0.0915 47  LEU B CB  
2609 C  CG  . LEU B 47  ? 0.2609 0.3842 0.5705 -0.0044 0.0782  -0.1311 47  LEU B CG  
2610 C  CD1 . LEU B 47  ? 0.0120 0.6194 1.0353 -0.0585 0.0071  0.0141  47  LEU B CD1 
2611 C  CD2 . LEU B 47  ? 0.1890 0.3115 0.5582 0.0972  0.0151  -0.0227 47  LEU B CD2 
2612 N  N   . SER B 48  ? 0.0184 0.2503 0.3825 -0.0487 -0.0326 0.0145  48  SER B N   
2613 C  CA  . SER B 48  ? 0.0147 0.2229 0.2915 -0.0337 -0.0141 -0.0475 48  SER B CA  
2614 C  C   . SER B 48  ? 0.0220 0.2549 0.3121 -0.0624 0.0188  -0.0788 48  SER B C   
2615 O  O   . SER B 48  ? 0.0439 0.2405 0.3170 -0.0925 0.0109  -0.0701 48  SER B O   
2616 C  CB  . SER B 48  ? 0.0336 0.2145 0.3471 -0.0573 0.0066  -0.0396 48  SER B CB  
2617 O  OG  . SER B 48  ? 0.1254 0.2521 0.3768 0.0070  0.0011  -0.0182 48  SER B OG  
2618 N  N   . VAL B 49  ? 0.0572 0.2370 0.3058 -0.0944 -0.0093 -0.0530 49  VAL B N   
2619 C  CA  . VAL B 49  ? 0.0897 0.3468 0.2952 -0.1231 -0.0063 -0.0707 49  VAL B CA  
2620 C  C   . VAL B 49  ? 0.1062 0.2762 0.3327 -0.1288 -0.0221 -0.0390 49  VAL B C   
2621 O  O   . VAL B 49  ? 0.1618 0.4109 0.3358 -0.1970 -0.0707 -0.0067 49  VAL B O   
2622 C  CB  . VAL B 49  ? 0.4252 0.3834 0.3785 0.0055  0.2084  0.0554  49  VAL B CB  
2623 C  CG1 . VAL B 49  ? 0.3310 0.7839 0.5043 0.0110  0.2643  0.2482  49  VAL B CG1 
2624 C  CG2 . VAL B 49  ? 0.4311 0.3189 0.3698 0.0739  0.0593  -0.0307 49  VAL B CG2 
2625 N  N   . SER B 50  ? 0.1692 0.2230 0.3398 -0.1088 -0.0538 -0.0663 50  SER B N   
2626 C  CA  . SER B 50  ? 0.1580 0.2620 0.4387 -0.0410 -0.0687 -0.0735 50  SER B CA  
2627 C  C   . SER B 50  ? 0.0458 0.3256 0.4557 -0.0587 -0.0961 -0.0807 50  SER B C   
2628 O  O   . SER B 50  ? 0.0658 0.3407 0.4449 -0.1230 -0.0933 0.0396  50  SER B O   
2629 C  CB  . SER B 50  ? 0.2073 0.2606 0.6243 -0.0565 -0.0882 -0.1167 50  SER B CB  
2630 O  OG  . SER B 50  ? 0.3699 0.5288 0.6894 0.0120  0.0006  -0.1613 50  SER B OG  
2631 N  N   . TYR B 51  ? 0.1532 0.2244 0.4292 -0.0991 -0.0915 -0.0662 51  TYR B N   
2632 C  CA  . TYR B 51  ? 0.1533 0.3300 0.3966 -0.0769 -0.1225 -0.0499 51  TYR B CA  
2633 C  C   . TYR B 51  ? 0.2383 0.2920 0.3635 -0.0398 -0.0650 0.0417  51  TYR B C   
2634 O  O   . TYR B 51  ? 0.1513 0.3004 0.3787 -0.0381 -0.0884 0.0205  51  TYR B O   
2635 C  CB  . TYR B 51  ? 0.1463 0.3063 0.4259 -0.0841 -0.1808 -0.0142 51  TYR B CB  
2636 C  CG  . TYR B 51  ? 0.0967 0.2116 0.2736 -0.0839 -0.0968 -0.0151 51  TYR B CG  
2637 C  CD1 . TYR B 51  ? 0.0581 0.1999 0.2836 -0.0858 -0.0261 -0.0397 51  TYR B CD1 
2638 C  CD2 . TYR B 51  ? 0.0816 0.2094 0.2513 -0.0802 -0.0282 -0.0192 51  TYR B CD2 
2639 C  CE1 . TYR B 51  ? 0.1114 0.1807 0.2693 -0.0851 -0.0856 -0.0322 51  TYR B CE1 
2640 C  CE2 . TYR B 51  ? 0.0863 0.1945 0.2338 -0.1021 -0.0499 -0.0428 51  TYR B CE2 
2641 C  CZ  . TYR B 51  ? 0.0834 0.1825 0.2723 -0.0762 -0.0828 -0.0518 51  TYR B CZ  
2642 O  OH  . TYR B 51  ? 0.1199 0.1442 0.2432 -0.0514 -0.0732 -0.0589 51  TYR B OH  
2643 N  N   . ASP B 52  ? 0.3749 0.3951 0.6424 0.0049  -0.0795 0.1267  52  ASP B N   
2644 C  CA  . ASP B 52  ? 0.2823 0.4713 0.5877 0.0980  -0.0281 0.1256  52  ASP B CA  
2645 C  C   . ASP B 52  ? 0.5193 0.2727 0.5127 -0.1243 -0.0804 -0.0048 52  ASP B C   
2646 O  O   . ASP B 52  ? 0.3931 0.4647 0.5256 -0.1272 -0.1896 0.1512  52  ASP B O   
2647 C  CB  . ASP B 52  ? 0.1280 0.5256 0.6582 -0.0341 -0.0621 0.1228  52  ASP B CB  
2648 C  CG  . ASP B 52  ? 0.4011 0.8707 0.8637 0.1068  -0.3055 -0.0514 52  ASP B CG  
2649 O  OD1 . ASP B 52  ? 0.7693 0.5118 1.0218 0.2866  0.0215  -0.0823 52  ASP B OD1 
2650 O  OD2 . ASP B 52  ? 0.7671 0.9619 1.2919 0.3058  0.0244  0.2198  52  ASP B OD2 
2651 N  N   . GLN B 53  ? 0.1524 0.2958 0.6736 -0.0512 -0.1483 0.0809  53  GLN B N   
2652 C  CA  . GLN B 53  ? 0.2123 0.4171 0.5590 -0.0264 -0.0106 0.0491  53  GLN B CA  
2653 C  C   . GLN B 53  ? 0.1945 0.2337 0.3498 -0.0234 -0.0614 -0.0185 53  GLN B C   
2654 O  O   . GLN B 53  ? 0.3095 0.2260 0.4475 -0.1134 -0.1782 0.0229  53  GLN B O   
2655 C  CB  . GLN B 53  ? 0.3261 0.4153 0.8162 -0.0595 -0.1148 0.0308  53  GLN B CB  
2656 C  CG  . GLN B 53  ? 0.3114 0.5769 0.8233 0.0054  -0.2045 0.0536  53  GLN B CG  
2657 C  CD  . GLN B 53  ? 0.1515 0.7297 1.0663 -0.0359 -0.2351 -0.0510 53  GLN B CD  
2658 O  OE1 . GLN B 53  ? 0.2383 1.0026 1.2107 -0.0174 -0.3426 0.2630  53  GLN B OE1 
2659 N  NE2 . GLN B 53  ? 0.1857 0.7291 0.8887 0.0077  -0.0467 0.1645  53  GLN B NE2 
2660 N  N   . ALA B 54  ? 0.1842 0.2245 0.4254 -0.0568 -0.1347 -0.0105 54  ALA B N   
2661 C  CA  . ALA B 54  ? 0.2055 0.1711 0.2638 -0.0735 -0.0943 -0.0625 54  ALA B CA  
2662 C  C   . ALA B 54  ? 0.3501 0.2070 0.2635 -0.0722 -0.1340 -0.0637 54  ALA B C   
2663 O  O   . ALA B 54  ? 0.3295 0.2760 0.3143 -0.1356 -0.1492 -0.0460 54  ALA B O   
2664 C  CB  . ALA B 54  ? 0.2499 0.2007 0.4366 -0.0206 -0.0804 -0.0538 54  ALA B CB  
2665 N  N   . THR B 55  ? 0.2883 0.1944 0.2931 -0.0551 -0.1567 -0.0439 55  THR B N   
2666 C  CA  . THR B 55  ? 0.3057 0.1638 0.2581 -0.0502 -0.1644 -0.0334 55  THR B CA  
2667 C  C   . THR B 55  ? 0.3888 0.1215 0.2442 -0.0219 -0.1289 0.0097  55  THR B C   
2668 O  O   . THR B 55  ? 0.4322 0.1305 0.2324 -0.0430 -0.1165 -0.0418 55  THR B O   
2669 C  CB  . THR B 55  ? 0.4811 0.1839 0.3656 -0.0065 -0.1088 0.0460  55  THR B CB  
2670 O  OG1 . THR B 55  ? 0.4500 0.1719 0.3554 -0.0500 -0.1228 -0.0572 55  THR B OG1 
2671 C  CG2 . THR B 55  ? 0.4567 0.1941 0.3602 0.0570  -0.0929 -0.0047 55  THR B CG2 
2672 N  N   . SER B 56  ? 0.3870 0.1491 0.2212 -0.0517 -0.0978 -0.0253 56  SER B N   
2673 C  CA  . SER B 56  ? 0.2558 0.1836 0.2422 -0.0889 -0.0943 -0.0143 56  SER B CA  
2674 C  C   . SER B 56  ? 0.1071 0.2488 0.2751 -0.0198 -0.0439 -0.0267 56  SER B C   
2675 O  O   . SER B 56  ? 0.1209 0.2396 0.2336 -0.0164 -0.0167 0.0092  56  SER B O   
2676 C  CB  . SER B 56  ? 0.3628 0.1892 0.2368 -0.0981 -0.1617 -0.0322 56  SER B CB  
2677 O  OG  . SER B 56  ? 0.4899 0.1614 0.2390 -0.0664 -0.2031 -0.0252 56  SER B OG  
2678 N  N   . LEU B 57  ? 0.0983 0.1612 0.1574 -0.0348 -0.0425 0.0046  57  LEU B N   
2679 C  CA  . LEU B 57  ? 0.0432 0.2394 0.2595 -0.0483 0.0509  0.0089  57  LEU B CA  
2680 C  C   . LEU B 57  ? 0.0681 0.2552 0.1942 0.0055  0.0418  0.0439  57  LEU B C   
2681 O  O   . LEU B 57  ? 0.1621 0.1856 0.1659 -0.0036 0.0080  0.0097  57  LEU B O   
2682 C  CB  . LEU B 57  ? 0.1302 0.2232 0.2663 -0.0540 -0.0148 0.0140  57  LEU B CB  
2683 C  CG  . LEU B 57  ? 0.3872 0.2033 0.2185 -0.0044 -0.0685 -0.0666 57  LEU B CG  
2684 C  CD1 . LEU B 57  ? 0.4196 0.1931 0.2606 -0.0487 -0.0186 -0.0324 57  LEU B CD1 
2685 C  CD2 . LEU B 57  ? 0.3694 0.2039 0.2624 0.0216  -0.0587 -0.0408 57  LEU B CD2 
2686 N  N   B ARG B 58  ? 0.1307 0.2074 0.1775 -0.0089 -0.0134 -0.0333 58  ARG B N   
2687 N  N   C ARG B 58  ? 0.1176 0.2024 0.2026 0.0130  -0.0182 -0.0428 58  ARG B N   
2688 C  CA  B ARG B 58  ? 0.0766 0.2457 0.1841 -0.0409 0.0129  0.0358  58  ARG B CA  
2689 C  CA  C ARG B 58  ? 0.0524 0.2424 0.1807 -0.0001 0.0107  0.0340  58  ARG B CA  
2690 C  C   B ARG B 58  ? 0.2087 0.1804 0.1863 -0.0621 0.0137  0.0095  58  ARG B C   
2691 C  C   C ARG B 58  ? 0.0949 0.1926 0.1518 -0.0893 -0.0211 0.0172  58  ARG B C   
2692 O  O   B ARG B 58  ? 0.1193 0.1550 0.1672 -0.0768 -0.0293 -0.0136 58  ARG B O   
2693 O  O   C ARG B 58  ? 0.0951 0.1921 0.1688 -0.0201 0.0055  -0.0083 58  ARG B O   
2694 C  CB  B ARG B 58  ? 0.0633 0.2948 0.2019 -0.0438 0.0941  0.0190  58  ARG B CB  
2695 C  CB  C ARG B 58  ? 0.0441 0.3182 0.1957 -0.0194 0.0130  0.0298  58  ARG B CB  
2696 C  CG  B ARG B 58  ? 0.0378 0.2151 0.2081 -0.0782 0.0354  -0.0404 58  ARG B CG  
2697 C  CG  C ARG B 58  ? 0.0664 0.1544 0.2466 -0.0791 0.0398  0.0048  58  ARG B CG  
2698 C  CD  B ARG B 58  ? 0.0263 0.2042 0.2628 -0.0500 0.0482  -0.0202 58  ARG B CD  
2699 C  CD  C ARG B 58  ? 0.0719 0.1970 0.1826 -0.1030 0.0244  -0.0168 58  ARG B CD  
2700 N  NE  B ARG B 58  ? 0.0289 0.1943 0.2749 -0.0617 0.0392  -0.0454 58  ARG B NE  
2701 N  NE  C ARG B 58  ? 0.0084 0.2164 0.2109 -0.0181 0.0133  -0.0294 58  ARG B NE  
2702 C  CZ  B ARG B 58  ? 0.0746 0.1816 0.2901 -0.0584 0.0794  0.0869  58  ARG B CZ  
2703 C  CZ  C ARG B 58  ? 0.0232 0.2630 0.2189 -0.0559 0.0113  0.0830  58  ARG B CZ  
2704 N  NH1 B ARG B 58  ? 0.0405 0.2902 0.3059 -0.0524 0.0644  0.0917  58  ARG B NH1 
2705 N  NH1 C ARG B 58  ? 0.0976 0.1462 0.1716 -0.0872 0.0245  -0.0311 58  ARG B NH1 
2706 N  NH2 B ARG B 58  ? 0.0972 0.4041 0.9325 -0.1888 -0.0741 0.0874  58  ARG B NH2 
2707 N  NH2 C ARG B 58  ? 0.0549 0.2086 0.2273 -0.0504 0.0359  0.0252  58  ARG B NH2 
2708 N  N   . ILE B 59  ? 0.2352 0.2311 0.1756 -0.0510 0.0153  -0.0444 59  ILE B N   
2709 C  CA  . ILE B 59  ? 0.0967 0.4525 0.3777 -0.2000 -0.0856 0.1582  59  ILE B CA  
2710 C  C   . ILE B 59  ? 0.3307 0.6672 0.2512 -0.4564 0.0181  -0.0929 59  ILE B C   
2711 O  O   . ILE B 59  ? 0.4610 0.2151 0.1680 -0.0288 -0.0374 -0.0621 59  ILE B O   
2712 C  CB  . ILE B 59  ? 0.0315 0.1948 0.3050 -0.0658 0.0236  0.0066  59  ILE B CB  
2713 C  CG1 . ILE B 59  ? 0.3726 0.2379 0.2237 -0.0153 0.0037  0.0092  59  ILE B CG1 
2714 C  CG2 . ILE B 59  ? 0.3643 0.1852 0.1857 -0.0547 -0.0906 -0.0752 59  ILE B CG2 
2715 C  CD1 . ILE B 59  ? 0.4044 0.1739 0.2977 -0.0141 0.0331  -0.0182 59  ILE B CD1 
2716 N  N   . LEU B 60  ? 0.0463 0.3435 0.3041 -0.0898 -0.0514 -0.0612 60  LEU B N   
2717 C  CA  . LEU B 60  ? 0.0379 0.2302 0.1472 -0.0744 -0.0194 -0.0040 60  LEU B CA  
2718 C  C   . LEU B 60  ? 0.2960 0.1967 0.1604 -0.0710 -0.0359 -0.0348 60  LEU B C   
2719 O  O   . LEU B 60  ? 0.1142 0.2199 0.1601 -0.0646 -0.0064 -0.0522 60  LEU B O   
2720 C  CB  . LEU B 60  ? 0.0699 0.2703 0.3068 0.0074  0.0160  -0.0319 60  LEU B CB  
2721 C  CG  . LEU B 60  ? 0.0498 0.1731 0.2237 -0.0078 0.0540  -0.0106 60  LEU B CG  
2722 C  CD1 . LEU B 60  ? 0.0150 0.4035 0.2920 -0.0524 0.0171  0.0375  60  LEU B CD1 
2723 C  CD2 . LEU B 60  ? 0.2073 0.2954 0.2560 0.0538  0.0025  -0.0331 60  LEU B CD2 
2724 N  N   . ASN B 61  ? 0.2688 0.2010 0.1481 -0.1252 -0.0027 -0.0087 61  ASN B N   
2725 C  CA  . ASN B 61  ? 0.3157 0.1454 0.1701 -0.1219 -0.0247 -0.1007 61  ASN B CA  
2726 C  C   . ASN B 61  ? 0.3755 0.1937 0.1634 -0.2151 -0.0294 -0.0509 61  ASN B C   
2727 O  O   . ASN B 61  ? 0.4709 0.1943 0.1771 -0.2241 0.0189  -0.0519 61  ASN B O   
2728 C  CB  . ASN B 61  ? 0.4009 0.1351 0.1908 -0.1430 0.0303  -0.0710 61  ASN B CB  
2729 C  CG  . ASN B 61  ? 0.3028 0.1572 0.1228 -0.1847 0.0499  -0.0650 61  ASN B CG  
2730 O  OD1 . ASN B 61  ? 0.3589 0.1757 0.1416 -0.1659 0.0211  -0.0617 61  ASN B OD1 
2731 N  ND2 . ASN B 61  ? 0.2830 0.1479 0.1500 -0.1583 0.0348  -0.0593 61  ASN B ND2 
2732 N  N   . ASN B 62  ? 0.4225 0.1356 0.1543 -0.1795 -0.0055 -0.0538 62  ASN B N   
2733 C  CA  . ASN B 62  ? 0.4172 0.2281 0.2206 -0.2487 0.0363  -0.0908 62  ASN B CA  
2734 C  C   . ASN B 62  ? 0.4228 0.2691 0.2022 -0.1614 0.0876  -0.0286 62  ASN B C   
2735 O  O   . ASN B 62  ? 0.4871 0.5333 0.1771 -0.2099 -0.0140 -0.0111 62  ASN B O   
2736 C  CB  . ASN B 62  ? 0.4856 0.1757 0.1846 -0.1499 -0.0001 -0.0602 62  ASN B CB  
2737 C  CG  . ASN B 62  ? 0.3799 0.2081 0.1554 -0.1134 -0.0638 -0.0502 62  ASN B CG  
2738 O  OD1 . ASN B 62  ? 0.2377 0.1684 0.1936 -0.1515 0.0243  -0.0739 62  ASN B OD1 
2739 N  ND2 . ASN B 62  ? 0.3943 0.1701 0.1970 -0.0969 -0.0684 -0.0546 62  ASN B ND2 
2740 N  N   . GLY B 63  ? 0.2577 0.2601 0.1717 -0.1346 0.0089  0.0201  63  GLY B N   
2741 C  CA  . GLY B 63  ? 0.1272 0.2599 0.2045 -0.1750 -0.0065 0.0078  63  GLY B CA  
2742 C  C   . GLY B 63  ? 0.2002 0.2244 0.2094 -0.0995 0.0204  -0.0462 63  GLY B C   
2743 O  O   . GLY B 63  ? 0.1118 0.2164 0.1701 -0.1228 0.0562  -0.0507 63  GLY B O   
2744 N  N   . HIS B 64  ? 0.2297 0.1879 0.1354 -0.1461 0.0096  -0.0532 64  HIS B N   
2745 C  CA  . HIS B 64  ? 0.1451 0.2260 0.1397 -0.1520 0.0330  -0.0438 64  HIS B CA  
2746 C  C   . HIS B 64  ? 0.1118 0.1925 0.1563 -0.1170 0.0084  -0.0579 64  HIS B C   
2747 O  O   . HIS B 64  ? 0.1421 0.2007 0.1795 -0.1285 0.0352  -0.0521 64  HIS B O   
2748 C  CB  . HIS B 64  ? 0.2119 0.2017 0.1486 -0.1526 0.0059  -0.0410 64  HIS B CB  
2749 C  CG  . HIS B 64  ? 0.1852 0.2509 0.1729 -0.1368 0.0401  -0.0376 64  HIS B CG  
2750 N  ND1 . HIS B 64  ? 0.1693 0.3015 0.2326 -0.1324 0.0387  -0.1190 64  HIS B ND1 
2751 C  CD2 . HIS B 64  ? 0.1687 0.2513 0.1966 -0.1198 0.0417  -0.0712 64  HIS B CD2 
2752 C  CE1 . HIS B 64  ? 0.2566 0.2325 0.2429 -0.1427 0.1119  -0.1257 64  HIS B CE1 
2753 N  NE2 . HIS B 64  ? 0.1635 0.2981 0.2891 -0.1404 0.0485  -0.1219 64  HIS B NE2 
2754 N  N   . SER B 65  ? 0.1150 0.1854 0.1706 -0.1305 -0.0131 -0.0299 65  SER B N   
2755 C  CA  . SER B 65  ? 0.0857 0.1564 0.1565 -0.1026 0.0200  -0.0467 65  SER B CA  
2756 C  C   . SER B 65  ? 0.1698 0.0857 0.1383 -0.0788 0.0263  -0.0565 65  SER B C   
2757 O  O   . SER B 65  ? 0.1914 0.1649 0.1508 -0.1298 0.0129  -0.0391 65  SER B O   
2758 C  CB  . SER B 65  ? 0.1288 0.1648 0.1486 -0.0825 0.0109  -0.0538 65  SER B CB  
2759 O  OG  . SER B 65  ? 0.1433 0.1859 0.2098 -0.1011 -0.0297 -0.0111 65  SER B OG  
2760 N  N   . PHE B 66  ? 0.1663 0.1040 0.1647 -0.0780 -0.0148 -0.0640 66  PHE B N   
2761 C  CA  . PHE B 66  ? 0.2200 0.1301 0.1276 -0.0623 -0.0201 -0.0486 66  PHE B CA  
2762 C  C   . PHE B 66  ? 0.2804 0.0894 0.1254 -0.0488 -0.0539 -0.0702 66  PHE B C   
2763 O  O   . PHE B 66  ? 0.2373 0.1091 0.1391 -0.0310 -0.0288 -0.0620 66  PHE B O   
2764 C  CB  . PHE B 66  ? 0.1845 0.1466 0.1527 -0.0548 -0.0374 -0.0526 66  PHE B CB  
2765 C  CG  . PHE B 66  ? 0.2184 0.1275 0.1338 -0.0802 -0.0265 -0.0581 66  PHE B CG  
2766 C  CD1 . PHE B 66  ? 0.2230 0.1429 0.1650 -0.0066 -0.0359 -0.0754 66  PHE B CD1 
2767 C  CD2 . PHE B 66  ? 0.2392 0.1383 0.1559 -0.0189 -0.0438 -0.0892 66  PHE B CD2 
2768 C  CE1 . PHE B 66  ? 0.2649 0.1443 0.1700 -0.0597 -0.0591 -0.0565 66  PHE B CE1 
2769 C  CE2 . PHE B 66  ? 0.2754 0.1578 0.1937 -0.0279 -0.0609 -0.0463 66  PHE B CE2 
2770 C  CZ  . PHE B 66  ? 0.2133 0.1465 0.1606 -0.0740 -0.0550 -0.0567 66  PHE B CZ  
2771 N  N   A GLN B 67  ? 0.0551 0.1341 0.1753 -0.0664 -0.0248 -0.0425 67  GLN B N   
2772 N  N   B GLN B 67  ? 0.1156 0.1107 0.1550 -0.0541 -0.0489 -0.0525 67  GLN B N   
2773 C  CA  A GLN B 67  ? 0.0553 0.1362 0.1652 -0.0721 -0.0156 -0.0369 67  GLN B CA  
2774 C  CA  B GLN B 67  ? 0.1323 0.1270 0.1451 -0.0271 -0.0346 -0.0486 67  GLN B CA  
2775 C  C   A GLN B 67  ? 0.0291 0.1184 0.1125 -0.0506 0.0265  -0.0574 67  GLN B C   
2776 C  C   B GLN B 67  ? 0.0561 0.1276 0.1530 0.0205  0.0309  -0.0582 67  GLN B C   
2777 O  O   A GLN B 67  ? 0.0154 0.1879 0.1040 -0.0387 0.0034  -0.0539 67  GLN B O   
2778 O  O   B GLN B 67  ? 0.1119 0.1837 0.1368 -0.0044 0.0184  -0.0661 67  GLN B O   
2779 C  CB  A GLN B 67  ? 0.0599 0.1486 0.1480 -0.0859 0.0221  -0.0605 67  GLN B CB  
2780 C  CB  B GLN B 67  ? 0.0309 0.1634 0.1366 -0.0480 0.0195  -0.0258 67  GLN B CB  
2781 C  CG  A GLN B 67  ? 0.0253 0.1657 0.1565 -0.0539 0.0237  -0.0407 67  GLN B CG  
2782 C  CG  B GLN B 67  ? 0.0160 0.1591 0.1524 -0.0264 0.0314  -0.0261 67  GLN B CG  
2783 C  CD  A GLN B 67  ? 0.0369 0.1329 0.1969 -0.0546 -0.0150 -0.0344 67  GLN B CD  
2784 C  CD  B GLN B 67  ? 0.0606 0.1439 0.2287 -0.0498 0.0021  -0.0174 67  GLN B CD  
2785 O  OE1 A GLN B 67  ? 0.0703 0.1374 0.2142 -0.0412 -0.0410 -0.0707 67  GLN B OE1 
2786 O  OE1 B GLN B 67  ? 0.1040 0.1597 0.2431 -0.0848 -0.0443 -0.0387 67  GLN B OE1 
2787 N  NE2 A GLN B 67  ? 0.1016 0.1174 0.2147 -0.0851 0.0004  -0.0609 67  GLN B NE2 
2788 N  NE2 B GLN B 67  ? 0.0444 0.1567 0.2408 -0.0737 0.0195  -0.0085 67  GLN B NE2 
2789 N  N   A VAL B 68  ? 0.0107 0.1117 0.1438 -0.0215 0.0121  -0.0585 68  VAL B N   
2790 N  N   B VAL B 68  ? 0.0195 0.0906 0.1548 0.0074  -0.0038 -0.0561 68  VAL B N   
2791 C  CA  A VAL B 68  ? 0.0116 0.1244 0.1116 -0.0236 0.0025  -0.0473 68  VAL B CA  
2792 C  CA  B VAL B 68  ? 0.0074 0.1151 0.1693 -0.0065 -0.0062 -0.0564 68  VAL B CA  
2793 C  C   A VAL B 68  ? 0.0073 0.1163 0.1163 -0.0103 0.0007  -0.0345 68  VAL B C   
2794 C  C   B VAL B 68  ? 0.0084 0.1282 0.1265 0.0002  -0.0146 -0.0507 68  VAL B C   
2795 O  O   A VAL B 68  ? 0.0116 0.1375 0.1251 -0.0195 -0.0113 -0.0322 68  VAL B O   
2796 O  O   B VAL B 68  ? 0.0644 0.0884 0.1198 -0.0491 -0.0230 -0.0455 68  VAL B O   
2797 C  CB  A VAL B 68  ? 0.0147 0.0961 0.1328 -0.0242 0.0264  -0.0579 68  VAL B CB  
2798 C  CB  B VAL B 68  ? 0.0121 0.1264 0.1396 -0.0201 0.0214  -0.0500 68  VAL B CB  
2799 C  CG1 A VAL B 68  ? 0.0231 0.1110 0.2107 -0.0414 0.0299  -0.0563 68  VAL B CG1 
2800 C  CG1 B VAL B 68  ? 0.0229 0.1292 0.2391 -0.0424 -0.0001 -0.0572 68  VAL B CG1 
2801 C  CG2 A VAL B 68  ? 0.0195 0.1057 0.1246 -0.0363 0.0241  -0.0641 68  VAL B CG2 
2802 C  CG2 B VAL B 68  ? 0.1005 0.1348 0.1369 -0.0026 0.0414  -0.0533 68  VAL B CG2 
2803 N  N   A GLU B 69  ? 0.0219 0.1183 0.1253 -0.0412 0.0034  -0.0261 69  GLU B N   
2804 N  N   B GLU B 69  ? 0.0237 0.1464 0.1601 -0.0489 0.0067  -0.0363 69  GLU B N   
2805 C  CA  A GLU B 69  ? 0.0280 0.1499 0.1303 -0.0535 0.0046  -0.0488 69  GLU B CA  
2806 C  CA  B GLU B 69  ? 0.0305 0.1674 0.1713 -0.0378 0.0141  -0.0624 69  GLU B CA  
2807 C  C   A GLU B 69  ? 0.0348 0.1138 0.1183 -0.0535 -0.0001 -0.0275 69  GLU B C   
2808 C  C   B GLU B 69  ? 0.0361 0.2223 0.1822 -0.0774 -0.0145 -0.0114 69  GLU B C   
2809 O  O   A GLU B 69  ? 0.0375 0.1170 0.1094 -0.0331 0.0060  -0.0365 69  GLU B O   
2810 O  O   B GLU B 69  ? 0.0477 0.1466 0.1545 -0.0132 -0.0306 -0.0403 69  GLU B O   
2811 C  CB  A GLU B 69  ? 0.0194 0.1936 0.1727 -0.0406 0.0355  -0.0448 69  GLU B CB  
2812 C  CB  B GLU B 69  ? 0.0231 0.1904 0.2167 -0.0506 -0.0068 -0.0344 69  GLU B CB  
2813 C  CG  A GLU B 69  ? 0.0127 0.2498 0.1808 -0.0356 0.0166  -0.0158 69  GLU B CG  
2814 C  CG  B GLU B 69  ? 0.0161 0.2062 0.2306 -0.0382 0.0313  -0.0433 69  GLU B CG  
2815 C  CD  A GLU B 69  ? 0.0937 0.1421 0.1378 -0.0405 0.0368  -0.0265 69  GLU B CD  
2816 C  CD  B GLU B 69  ? 0.0210 0.2511 0.1839 -0.0582 0.0256  -0.0590 69  GLU B CD  
2817 O  OE1 A GLU B 69  ? 0.1235 0.1324 0.1631 -0.0395 0.0209  -0.0348 69  GLU B OE1 
2818 O  OE1 B GLU B 69  ? 0.0272 0.2435 0.1925 -0.0440 0.0058  -0.0406 69  GLU B OE1 
2819 O  OE2 A GLU B 69  ? 0.0811 0.1778 0.1841 -0.0588 0.0447  -0.0179 69  GLU B OE2 
2820 O  OE2 B GLU B 69  ? 0.1335 0.2095 0.2010 -0.0141 0.0731  -0.0158 69  GLU B OE2 
2821 N  N   . PHE B 70  ? 0.2530 0.1190 0.1524 -0.0332 -0.0306 -0.0438 70  PHE B N   
2822 C  CA  . PHE B 70  ? 0.2179 0.1150 0.2017 -0.0660 -0.0908 -0.0307 70  PHE B CA  
2823 C  C   . PHE B 70  ? 0.3182 0.1119 0.2533 -0.0571 -0.0945 -0.0252 70  PHE B C   
2824 O  O   . PHE B 70  ? 0.2903 0.1175 0.2166 -0.0719 -0.0384 -0.0316 70  PHE B O   
2825 C  CB  . PHE B 70  ? 0.2272 0.1156 0.1893 -0.0335 -0.0889 -0.0524 70  PHE B CB  
2826 C  CG  . PHE B 70  ? 0.2801 0.1262 0.1912 -0.0510 -0.1279 -0.0291 70  PHE B CG  
2827 C  CD1 . PHE B 70  ? 0.2275 0.1204 0.2051 -0.0498 -0.1102 -0.0271 70  PHE B CD1 
2828 C  CD2 . PHE B 70  ? 0.2649 0.0924 0.1837 -0.0451 -0.1051 -0.0702 70  PHE B CD2 
2829 C  CE1 . PHE B 70  ? 0.2661 0.1240 0.2505 -0.0550 -0.1293 -0.0466 70  PHE B CE1 
2830 C  CE2 . PHE B 70  ? 0.2309 0.1035 0.2307 -0.0550 -0.0945 -0.0363 70  PHE B CE2 
2831 C  CZ  . PHE B 70  ? 0.2648 0.1719 0.2027 -0.0289 -0.0718 -0.0030 70  PHE B CZ  
2832 N  N   . ASP B 71  ? 0.3641 0.1308 0.2382 -0.0585 -0.1160 -0.0187 71  ASP B N   
2833 C  CA  . ASP B 71  ? 0.3125 0.1329 0.2210 -0.0901 -0.0829 -0.0074 71  ASP B CA  
2834 C  C   . ASP B 71  ? 0.2781 0.1397 0.2386 -0.0228 -0.0970 -0.0326 71  ASP B C   
2835 O  O   . ASP B 71  ? 0.3922 0.1729 0.3247 -0.0993 -0.0424 -0.0604 71  ASP B O   
2836 C  CB  . ASP B 71  ? 0.2987 0.1591 0.3212 -0.0126 -0.0591 0.0174  71  ASP B CB  
2837 C  CG  . ASP B 71  ? 0.3911 0.1869 0.3300 -0.0083 -0.1536 -0.0597 71  ASP B CG  
2838 O  OD1 . ASP B 71  ? 0.2464 0.2145 0.3331 -0.0480 -0.0563 0.0336  71  ASP B OD1 
2839 O  OD2 . ASP B 71  ? 0.3471 0.2116 0.4496 -0.0637 -0.1302 -0.0454 71  ASP B OD2 
2840 N  N   . ASP B 72  ? 0.2811 0.1307 0.2471 -0.0413 -0.0903 -0.0524 72  ASP B N   
2841 C  CA  . ASP B 72  ? 0.2477 0.0952 0.2612 -0.0212 -0.0556 -0.0617 72  ASP B CA  
2842 C  C   . ASP B 72  ? 0.1698 0.1021 0.3330 -0.0555 -0.0873 -0.0693 72  ASP B C   
2843 O  O   . ASP B 72  ? 0.2500 0.1762 0.2655 -0.0719 -0.0588 -0.0436 72  ASP B O   
2844 C  CB  . ASP B 72  ? 0.2445 0.1224 0.2649 -0.0331 -0.0704 -0.0362 72  ASP B CB  
2845 C  CG  . ASP B 72  ? 0.3116 0.1936 0.2879 -0.0734 -0.0462 0.0441  72  ASP B CG  
2846 O  OD1 . ASP B 72  ? 0.3946 0.2812 0.2324 -0.0582 -0.0568 0.0088  72  ASP B OD1 
2847 O  OD2 . ASP B 72  ? 0.3148 0.2453 0.2427 -0.0110 -0.0314 -0.0148 72  ASP B OD2 
2848 N  N   . SER B 73  ? 0.2046 0.1345 0.3652 -0.0446 -0.0877 -0.0205 73  SER B N   
2849 C  CA  . SER B 73  ? 0.2865 0.1351 0.3138 -0.0886 -0.0616 -0.0752 73  SER B CA  
2850 C  C   . SER B 73  ? 0.4020 0.1244 0.3172 -0.0576 0.0104  -0.0538 73  SER B C   
2851 O  O   . SER B 73  ? 0.5195 0.1213 0.3453 -0.0328 -0.0563 -0.0434 73  SER B O   
2852 C  CB  . SER B 73  ? 0.2700 0.2331 0.3094 -0.0771 -0.0166 -0.0791 73  SER B CB  
2853 O  OG  . SER B 73  ? 0.3213 0.1464 0.3490 -0.0279 -0.0846 -0.0456 73  SER B OG  
2854 N  N   . GLN B 74  ? 0.2816 0.2239 0.3512 -0.0196 0.0252  -0.0257 74  GLN B N   
2855 C  CA  . GLN B 74  ? 0.2473 0.2355 0.3883 0.0186  -0.0211 -0.0198 74  GLN B CA  
2856 C  C   . GLN B 74  ? 0.2554 0.2214 0.2888 -0.0491 -0.1277 -0.0795 74  GLN B C   
2857 O  O   . GLN B 74  ? 0.2035 0.2096 0.3336 -0.0673 -0.0423 -0.0903 74  GLN B O   
2858 C  CB  . GLN B 74  ? 0.3374 0.3077 0.5035 0.0392  -0.0926 -0.0173 74  GLN B CB  
2859 C  CG  . GLN B 74  ? 0.4149 0.5256 0.5381 -0.1340 -0.1262 0.0554  74  GLN B CG  
2860 C  CD  . GLN B 74  ? 0.2825 0.5425 0.5681 -0.0670 -0.0194 0.0516  74  GLN B CD  
2861 O  OE1 . GLN B 74  ? 0.1820 0.8083 0.6822 -0.0399 -0.0729 0.1224  74  GLN B OE1 
2862 N  NE2 . GLN B 74  ? 0.1972 0.4663 0.5594 -0.0250 -0.0653 0.0343  74  GLN B NE2 
2863 N  N   . ASP B 75  ? 0.2918 0.2336 0.3074 -0.0305 -0.0702 -0.0491 75  ASP B N   
2864 C  CA  . ASP B 75  ? 0.2477 0.2542 0.3432 -0.0641 -0.0851 -0.0446 75  ASP B CA  
2865 C  C   . ASP B 75  ? 0.2763 0.2608 0.3903 -0.0074 -0.1003 -0.1229 75  ASP B C   
2866 O  O   . ASP B 75  ? 0.3277 0.4371 0.7197 0.0277  -0.2160 -0.0540 75  ASP B O   
2867 C  CB  . ASP B 75  ? 0.2408 0.2976 0.4339 0.0039  -0.0770 -0.1248 75  ASP B CB  
2868 C  CG  . ASP B 75  ? 0.2144 0.3330 0.3611 0.0461  -0.0686 -0.0845 75  ASP B CG  
2869 O  OD1 . ASP B 75  ? 0.2708 0.4700 0.3666 0.0901  -0.1049 -0.1859 75  ASP B OD1 
2870 O  OD2 . ASP B 75  ? 0.4519 0.4986 0.5281 0.0005  0.1062  -0.1801 75  ASP B OD2 
2871 N  N   . LYS B 76  ? 0.1879 0.1736 0.3856 -0.0525 -0.0892 -0.0158 76  LYS B N   
2872 C  CA  . LYS B 76  ? 0.2056 0.1768 0.4132 -0.1185 -0.0163 -0.0359 76  LYS B CA  
2873 C  C   . LYS B 76  ? 0.0721 0.2934 0.6980 -0.1204 -0.1525 0.1299  76  LYS B C   
2874 O  O   . LYS B 76  ? 0.3471 0.3893 0.8797 -0.0447 0.0841  0.1732  76  LYS B O   
2875 C  CB  . LYS B 76  ? 0.3124 0.2727 0.3608 -0.0522 -0.0052 0.0070  76  LYS B CB  
2876 C  CG  . LYS B 76  ? 0.3607 0.2799 0.3358 -0.1479 -0.0641 0.0196  76  LYS B CG  
2877 C  CD  . LYS B 76  ? 0.5489 0.3309 0.3134 -0.1667 -0.0776 -0.0008 76  LYS B CD  
2878 C  CE  . LYS B 76  ? 0.4689 0.3282 0.2842 -0.1625 -0.1428 -0.0472 76  LYS B CE  
2879 N  NZ  . LYS B 76  ? 0.4375 0.2438 0.3177 -0.0094 -0.0907 -0.0441 76  LYS B NZ  
2880 N  N   . ALA B 77  ? 0.2136 0.2848 0.3884 -0.0054 -0.1315 0.0603  77  ALA B N   
2881 C  CA  . ALA B 77  ? 0.2210 0.1691 0.3265 -0.0259 -0.1408 -0.0340 77  ALA B CA  
2882 C  C   . ALA B 77  ? 0.1149 0.2602 0.3100 -0.0536 -0.1297 0.0541  77  ALA B C   
2883 O  O   . ALA B 77  ? 0.0966 0.2938 0.3287 -0.0221 -0.0827 -0.0512 77  ALA B O   
2884 C  CB  . ALA B 77  ? 0.2803 0.2444 0.3161 0.0596  -0.1967 -0.0993 77  ALA B CB  
2885 N  N   . VAL B 78  ? 0.0579 0.2412 0.3025 -0.0542 -0.1069 -0.0033 78  VAL B N   
2886 C  CA  . VAL B 78  ? 0.0888 0.1938 0.2913 -0.0454 -0.0827 -0.0242 78  VAL B CA  
2887 C  C   . VAL B 78  ? 0.0370 0.2017 0.2360 -0.0477 -0.0445 -0.0477 78  VAL B C   
2888 O  O   . VAL B 78  ? 0.0660 0.2115 0.3492 -0.0700 -0.0699 -0.0629 78  VAL B O   
2889 C  CB  . VAL B 78  ? 0.0906 0.2480 0.3445 -0.0643 -0.0571 -0.0666 78  VAL B CB  
2890 C  CG1 . VAL B 78  ? 0.2597 0.1506 0.3499 0.0032  -0.0668 -0.0624 78  VAL B CG1 
2891 C  CG2 . VAL B 78  ? 0.1265 0.2816 0.3393 0.0084  0.0163  -0.0939 78  VAL B CG2 
2892 N  N   . LEU B 79  ? 0.0658 0.1416 0.2467 -0.0361 -0.0582 -0.0345 79  LEU B N   
2893 C  CA  . LEU B 79  ? 0.0205 0.1843 0.2341 -0.0421 -0.0189 -0.0482 79  LEU B CA  
2894 C  C   . LEU B 79  ? 0.0280 0.1997 0.2564 -0.0545 -0.0175 -0.0521 79  LEU B C   
2895 O  O   . LEU B 79  ? 0.0349 0.1998 0.2737 -0.0664 -0.0083 -0.0592 79  LEU B O   
2896 C  CB  . LEU B 79  ? 0.0241 0.1603 0.3010 -0.0496 -0.0109 -0.0350 79  LEU B CB  
2897 C  CG  . LEU B 79  ? 0.0168 0.1925 0.3046 -0.0299 -0.0062 -0.0164 79  LEU B CG  
2898 C  CD1 . LEU B 79  ? 0.0851 0.1372 0.4316 -0.0611 0.0192  -0.0039 79  LEU B CD1 
2899 C  CD2 . LEU B 79  ? 0.0397 0.1740 0.2547 -0.0196 0.0226  -0.0610 79  LEU B CD2 
2900 N  N   . LYS B 80  ? 0.0500 0.2076 0.2684 -0.0509 0.0140  -0.0642 80  LYS B N   
2901 C  CA  . LYS B 80  ? 0.0699 0.2066 0.2532 -0.0458 0.0219  -0.0372 80  LYS B CA  
2902 C  C   . LYS B 80  ? 0.0394 0.1864 0.2657 -0.0451 0.0195  -0.0521 80  LYS B C   
2903 O  O   . LYS B 80  ? 0.0371 0.2204 0.3676 -0.0804 0.0108  -0.0636 80  LYS B O   
2904 C  CB  . LYS B 80  ? 0.2261 0.2120 0.2908 0.0116  0.0759  -0.0226 80  LYS B CB  
2905 C  CG  . LYS B 80  ? 0.1650 0.2931 0.4080 -0.0058 0.0774  0.0678  80  LYS B CG  
2906 C  CD  . LYS B 80  ? 0.2011 0.3716 0.6379 0.0417  -0.0544 -0.0444 80  LYS B CD  
2907 C  CE  . LYS B 80  ? 0.3207 0.4781 0.7864 0.1314  0.0128  0.0207  80  LYS B CE  
2908 N  NZ  . LYS B 80  ? 0.3298 0.5468 0.6912 0.1346  -0.0060 -0.0248 80  LYS B NZ  
2909 N  N   . GLY B 81  ? 0.0833 0.1734 0.2967 -0.0251 0.0516  -0.0487 81  GLY B N   
2910 C  CA  . GLY B 81  ? 0.0312 0.2018 0.3741 -0.0368 0.0868  -0.0329 81  GLY B CA  
2911 C  C   . GLY B 81  ? 0.0229 0.1666 0.3736 -0.0425 0.0529  -0.0596 81  GLY B C   
2912 O  O   . GLY B 81  ? 0.0305 0.1736 0.2753 -0.0609 0.0347  -0.0704 81  GLY B O   
2913 N  N   . GLY B 82  ? 0.0928 0.1964 0.4246 -0.0187 0.0776  0.0108  82  GLY B N   
2914 C  CA  . GLY B 82  ? 0.0861 0.2062 0.5148 -0.0341 0.0862  0.0486  82  GLY B CA  
2915 C  C   . GLY B 82  ? 0.1087 0.2509 0.3829 0.0659  0.0965  0.0334  82  GLY B C   
2916 O  O   . GLY B 82  ? 0.3164 0.3956 0.3991 0.1097  0.1342  0.0370  82  GLY B O   
2917 N  N   . PRO B 83  ? 0.0881 0.2262 0.3086 -0.0032 0.0897  -0.0414 83  PRO B N   
2918 C  CA  . PRO B 83  ? 0.1247 0.2131 0.2169 0.0080  0.0913  -0.0265 83  PRO B CA  
2919 C  C   . PRO B 83  ? 0.1166 0.1965 0.2131 0.0042  0.0482  -0.0627 83  PRO B C   
2920 O  O   . PRO B 83  ? 0.1498 0.3239 0.2678 0.0267  0.0071  -0.1079 83  PRO B O   
2921 C  CB  . PRO B 83  ? 0.1530 0.2129 0.2324 0.0157  0.0949  -0.0198 83  PRO B CB  
2922 C  CG  . PRO B 83  ? 0.0430 0.1985 0.2492 -0.0129 0.0220  -0.0545 83  PRO B CG  
2923 C  CD  . PRO B 83  ? 0.0239 0.1985 0.3073 0.0019  0.0535  -0.0604 83  PRO B CD  
2924 N  N   . LEU B 84  ? 0.0518 0.1739 0.2112 -0.0073 0.0463  -0.0583 84  LEU B N   
2925 C  CA  . LEU B 84  ? 0.0529 0.1642 0.2147 -0.0103 0.0299  -0.0630 84  LEU B CA  
2926 C  C   . LEU B 84  ? 0.0550 0.1987 0.2936 -0.0050 0.0265  -0.0961 84  LEU B C   
2927 O  O   . LEU B 84  ? 0.0588 0.2174 0.3380 0.0195  0.0403  -0.1145 84  LEU B O   
2928 C  CB  . LEU B 84  ? 0.0095 0.1852 0.2233 -0.0161 0.0253  -0.0890 84  LEU B CB  
2929 C  CG  . LEU B 84  ? 0.0121 0.1518 0.2172 -0.0134 0.0140  -0.0644 84  LEU B CG  
2930 C  CD1 . LEU B 84  ? 0.0333 0.2057 0.2246 -0.0046 -0.0027 -0.0718 84  LEU B CD1 
2931 C  CD2 . LEU B 84  ? 0.0117 0.1802 0.2287 -0.0102 0.0170  -0.0483 84  LEU B CD2 
2932 N  N   . ASP B 85  ? 0.0845 0.1992 0.2776 -0.0093 0.0648  -0.0956 85  ASP B N   
2933 C  CA  . ASP B 85  ? 0.1609 0.1899 0.3160 -0.0262 0.0168  -0.1221 85  ASP B CA  
2934 C  C   . ASP B 85  ? 0.1795 0.2155 0.3924 0.0135  0.1169  -0.0231 85  ASP B C   
2935 O  O   . ASP B 85  ? 0.1242 0.3613 0.4714 -0.0367 0.1002  -0.1658 85  ASP B O   
2936 C  CB  . ASP B 85  ? 0.4104 0.3732 0.4282 -0.0681 -0.1196 -0.2037 85  ASP B CB  
2937 C  CG  . ASP B 85  ? 0.3780 0.4239 0.5515 0.0662  -0.1602 -0.1268 85  ASP B CG  
2938 O  OD1 . ASP B 85  ? 0.8095 0.4004 0.7420 -0.1458 -0.1478 -0.1307 85  ASP B OD1 
2939 O  OD2 . ASP B 85  ? 0.4718 0.4005 0.6856 -0.0250 -0.2292 -0.1620 85  ASP B OD2 
2940 N  N   . GLY B 86  ? 0.2648 0.2560 0.3647 -0.0359 -0.0987 -0.1243 86  GLY B N   
2941 C  CA  . GLY B 86  ? 0.4062 0.2673 0.3209 -0.0979 0.0462  -0.1615 86  GLY B CA  
2942 C  C   . GLY B 86  ? 0.1676 0.2479 0.2828 -0.1576 -0.0132 -0.1043 86  GLY B C   
2943 O  O   . GLY B 86  ? 0.2208 0.2773 0.3397 -0.1655 -0.0036 -0.0542 86  GLY B O   
2944 N  N   . THR B 87  ? 0.0762 0.1858 0.2679 -0.0278 0.0005  -0.0791 87  THR B N   
2945 C  CA  . THR B 87  ? 0.0252 0.1615 0.2888 -0.0434 -0.0096 -0.0841 87  THR B CA  
2946 C  C   . THR B 87  ? 0.0210 0.1409 0.2650 -0.0318 -0.0177 -0.0857 87  THR B C   
2947 O  O   . THR B 87  ? 0.0596 0.1263 0.2652 -0.0458 0.0002  -0.0871 87  THR B O   
2948 C  CB  . THR B 87  ? 0.0743 0.3458 0.3143 0.0899  -0.0230 -0.0842 87  THR B CB  
2949 O  OG1 . THR B 87  ? 0.0613 0.3820 0.4817 -0.0006 0.0153  -0.1461 87  THR B OG1 
2950 C  CG2 . THR B 87  ? 0.1840 0.3415 0.3394 0.0603  -0.0691 -0.0906 87  THR B CG2 
2951 N  N   . TYR B 88  ? 0.0405 0.1191 0.2475 -0.0155 -0.0226 -0.0614 88  TYR B N   
2952 C  CA  . TYR B 88  ? 0.0279 0.1425 0.2321 -0.0436 -0.0167 -0.0667 88  TYR B CA  
2953 C  C   . TYR B 88  ? 0.0284 0.1434 0.2285 -0.0342 -0.0337 -0.0680 88  TYR B C   
2954 O  O   . TYR B 88  ? 0.0863 0.1693 0.2759 -0.0857 -0.0725 -0.0306 88  TYR B O   
2955 C  CB  . TYR B 88  ? 0.0640 0.1211 0.2249 -0.0512 -0.0375 -0.0602 88  TYR B CB  
2956 C  CG  . TYR B 88  ? 0.0310 0.1150 0.1972 -0.0312 0.0034  -0.0510 88  TYR B CG  
2957 C  CD1 . TYR B 88  ? 0.0209 0.1361 0.1963 -0.0289 0.0078  -0.0525 88  TYR B CD1 
2958 C  CD2 . TYR B 88  ? 0.0308 0.1053 0.1706 -0.0260 -0.0023 -0.0544 88  TYR B CD2 
2959 C  CE1 . TYR B 88  ? 0.0167 0.1511 0.1774 -0.0371 0.0251  -0.0527 88  TYR B CE1 
2960 C  CE2 . TYR B 88  ? 0.0207 0.1091 0.1734 -0.0331 0.0148  -0.0484 88  TYR B CE2 
2961 C  CZ  . TYR B 88  ? 0.0237 0.1078 0.1761 -0.0379 0.0017  -0.0598 88  TYR B CZ  
2962 O  OH  . TYR B 88  ? 0.0209 0.1527 0.1737 -0.0326 -0.0013 -0.0754 88  TYR B OH  
2963 N  N   . ARG B 89  ? 0.0363 0.1303 0.2071 -0.0289 -0.0200 -0.0754 89  ARG B N   
2964 C  CA  . ARG B 89  ? 0.1019 0.1269 0.2178 -0.0332 -0.0664 -0.0511 89  ARG B CA  
2965 C  C   . ARG B 89  ? 0.0488 0.1083 0.1714 -0.0408 -0.0512 -0.0309 89  ARG B C   
2966 O  O   . ARG B 89  ? 0.0420 0.1073 0.1788 -0.0381 -0.0389 -0.0388 89  ARG B O   
2967 C  CB  . ARG B 89  ? 0.0263 0.1828 0.3242 -0.0464 -0.0359 0.0035  89  ARG B CB  
2968 C  CG  . ARG B 89  ? 0.0974 0.2042 0.3262 -0.0163 -0.0270 -0.0152 89  ARG B CG  
2969 C  CD  . ARG B 89  ? 0.2449 0.2141 0.2971 -0.0162 -0.0990 0.0220  89  ARG B CD  
2970 N  NE  . ARG B 89  ? 0.2710 0.2590 0.2819 -0.0547 -0.0858 -0.0436 89  ARG B NE  
2971 C  CZ  . ARG B 89  ? 0.2776 0.2164 0.4098 0.0093  -0.0319 -0.0091 89  ARG B CZ  
2972 N  NH1 . ARG B 89  ? 0.2716 0.2508 0.3030 -0.0138 -0.0427 -0.0461 89  ARG B NH1 
2973 N  NH2 . ARG B 89  ? 0.3468 0.2545 0.4418 0.0399  0.0227  -0.0250 89  ARG B NH2 
2974 N  N   . LEU B 90  ? 0.0622 0.1165 0.1897 -0.0469 -0.0586 -0.0433 90  LEU B N   
2975 C  CA  . LEU B 90  ? 0.0818 0.1082 0.2042 -0.0414 -0.0704 -0.0590 90  LEU B CA  
2976 C  C   . LEU B 90  ? 0.1429 0.0981 0.2117 -0.0463 -0.0793 -0.0457 90  LEU B C   
2977 O  O   . LEU B 90  ? 0.1477 0.1485 0.1933 -0.0359 -0.0581 -0.0249 90  LEU B O   
2978 C  CB  . LEU B 90  ? 0.1139 0.1143 0.2396 -0.0355 -0.1174 -0.0618 90  LEU B CB  
2979 C  CG  . LEU B 90  ? 0.1495 0.1500 0.1931 -0.0679 -0.0813 -0.0744 90  LEU B CG  
2980 C  CD1 . LEU B 90  ? 0.2033 0.1240 0.2150 -0.0658 -0.0644 -0.0633 90  LEU B CD1 
2981 C  CD2 . LEU B 90  ? 0.1140 0.1760 0.2898 -0.0569 -0.0829 -0.0981 90  LEU B CD2 
2982 N  N   . LEU B 91  ? 0.1252 0.0893 0.1671 -0.0482 -0.0520 -0.0580 91  LEU B N   
2983 C  CA  . LEU B 91  ? 0.1405 0.1245 0.1643 -0.0309 -0.0440 -0.0487 91  LEU B CA  
2984 C  C   . LEU B 91  ? 0.1443 0.1085 0.1609 -0.0618 -0.0505 -0.0413 91  LEU B C   
2985 O  O   . LEU B 91  ? 0.1527 0.1073 0.1549 -0.0657 -0.0550 -0.0231 91  LEU B O   
2986 C  CB  . LEU B 91  ? 0.1493 0.1479 0.1946 -0.0391 -0.0403 -0.0912 91  LEU B CB  
2987 C  CG  . LEU B 91  ? 0.1483 0.1458 0.2063 -0.0643 -0.0509 -0.0670 91  LEU B CG  
2988 C  CD1 . LEU B 91  ? 0.2497 0.1631 0.4372 -0.0853 -0.0797 0.0424  91  LEU B CD1 
2989 C  CD2 . LEU B 91  ? 0.0820 0.2815 0.2957 -0.0533 -0.0267 -0.1112 91  LEU B CD2 
2990 N  N   . GLN B 92  ? 0.1864 0.0942 0.1421 -0.0584 -0.0440 -0.0484 92  GLN B N   
2991 C  CA  . GLN B 92  ? 0.2196 0.0911 0.1377 -0.0535 -0.0185 -0.0391 92  GLN B CA  
2992 C  C   . GLN B 92  ? 0.1034 0.0892 0.1240 -0.0502 -0.0032 -0.0418 92  GLN B C   
2993 O  O   . GLN B 92  ? 0.1495 0.1043 0.1252 -0.0548 -0.0263 -0.0355 92  GLN B O   
2994 C  CB  . GLN B 92  ? 0.2100 0.0869 0.1562 -0.0819 -0.0320 -0.0533 92  GLN B CB  
2995 C  CG  . GLN B 92  ? 0.1459 0.1405 0.2012 -0.0864 -0.0359 -0.0284 92  GLN B CG  
2996 C  CD  . GLN B 92  ? 0.2340 0.1718 0.2161 -0.0310 -0.0995 -0.0280 92  GLN B CD  
2997 O  OE1 . GLN B 92  ? 0.4904 0.1373 0.2719 -0.0472 -0.1696 -0.0373 92  GLN B OE1 
2998 N  NE2 . GLN B 92  ? 0.2014 0.3828 0.3026 -0.0207 -0.0964 -0.1833 92  GLN B NE2 
2999 N  N   . PHE B 93  ? 0.1509 0.0867 0.1495 -0.0521 -0.0362 -0.0442 93  PHE B N   
3000 C  CA  . PHE B 93  ? 0.1487 0.0849 0.1707 -0.0681 -0.0664 -0.0425 93  PHE B CA  
3001 C  C   . PHE B 93  ? 0.1773 0.1085 0.1270 -0.0726 -0.0542 -0.0370 93  PHE B C   
3002 O  O   . PHE B 93  ? 0.2051 0.1003 0.1218 -0.0419 -0.0434 -0.0321 93  PHE B O   
3003 C  CB  . PHE B 93  ? 0.1229 0.1098 0.1786 -0.0379 -0.0754 -0.0447 93  PHE B CB  
3004 C  CG  . PHE B 93  ? 0.1761 0.0924 0.1655 -0.0730 -0.0603 -0.0317 93  PHE B CG  
3005 C  CD1 . PHE B 93  ? 0.1744 0.1109 0.2042 -0.0895 -0.0765 -0.0555 93  PHE B CD1 
3006 C  CD2 . PHE B 93  ? 0.2455 0.1003 0.1896 -0.0425 -0.1124 -0.0418 93  PHE B CD2 
3007 C  CE1 . PHE B 93  ? 0.2410 0.1007 0.1902 -0.0804 -0.1093 -0.0403 93  PHE B CE1 
3008 C  CE2 . PHE B 93  ? 0.2813 0.1301 0.2021 -0.0611 -0.1338 -0.0247 93  PHE B CE2 
3009 C  CZ  . PHE B 93  ? 0.3125 0.1188 0.2267 -0.0480 -0.1414 -0.0328 93  PHE B CZ  
3010 N  N   . HIS B 94  ? 0.1288 0.0952 0.1324 -0.0485 -0.0529 -0.0562 94  HIS B N   
3011 C  CA  . HIS B 94  ? 0.0961 0.1005 0.1161 -0.0456 -0.0414 -0.0348 94  HIS B CA  
3012 C  C   . HIS B 94  ? 0.0673 0.0940 0.0992 -0.0527 -0.0227 -0.0396 94  HIS B C   
3013 O  O   . HIS B 94  ? 0.0861 0.0857 0.1193 -0.0469 -0.0030 -0.0445 94  HIS B O   
3014 C  CB  . HIS B 94  ? 0.1221 0.1054 0.1377 -0.0811 -0.0376 -0.0446 94  HIS B CB  
3015 C  CG  . HIS B 94  ? 0.0876 0.1051 0.1170 -0.0763 -0.0109 -0.0439 94  HIS B CG  
3016 N  ND1 . HIS B 94  ? 0.0709 0.0973 0.1274 -0.0666 -0.0147 -0.0359 94  HIS B ND1 
3017 C  CD2 . HIS B 94  ? 0.0784 0.1141 0.1107 -0.0785 -0.0046 -0.0429 94  HIS B CD2 
3018 C  CE1 . HIS B 94  ? 0.0585 0.0954 0.1277 -0.0535 -0.0100 -0.0275 94  HIS B CE1 
3019 N  NE2 . HIS B 94  ? 0.0443 0.1167 0.0746 -0.0521 -0.0230 -0.0139 94  HIS B NE2 
3020 N  N   . PHE B 95  ? 0.0754 0.0966 0.1331 -0.0521 -0.0199 -0.0407 95  PHE B N   
3021 C  CA  . PHE B 95  ? 0.0687 0.0936 0.1335 -0.0504 -0.0262 -0.0385 95  PHE B CA  
3022 C  C   . PHE B 95  ? 0.0527 0.0868 0.0903 -0.0491 0.0055  -0.0458 95  PHE B C   
3023 O  O   . PHE B 95  ? 0.0504 0.1274 0.1163 -0.0574 0.0055  -0.0324 95  PHE B O   
3024 C  CB  . PHE B 95  ? 0.0584 0.1107 0.1315 -0.0519 -0.0177 -0.0490 95  PHE B CB  
3025 C  CG  . PHE B 95  ? 0.0581 0.1028 0.1270 -0.0577 -0.0143 -0.0439 95  PHE B CG  
3026 C  CD1 . PHE B 95  ? 0.0982 0.0906 0.1411 -0.0552 -0.0285 -0.0576 95  PHE B CD1 
3027 C  CD2 . PHE B 95  ? 0.0667 0.1315 0.1436 -0.0718 -0.0129 -0.0577 95  PHE B CD2 
3028 C  CE1 . PHE B 95  ? 0.1061 0.1286 0.1378 -0.0334 -0.0228 -0.0538 95  PHE B CE1 
3029 C  CE2 . PHE B 95  ? 0.0705 0.1221 0.1492 -0.0600 -0.0259 -0.0647 95  PHE B CE2 
3030 C  CZ  . PHE B 95  ? 0.0588 0.1497 0.1394 -0.0420 -0.0405 -0.0704 95  PHE B CZ  
3031 N  N   . HIS B 96  ? 0.0748 0.0793 0.1228 -0.0526 -0.0133 -0.0507 96  HIS B N   
3032 C  CA  . HIS B 96  ? 0.0759 0.0848 0.1173 -0.0407 -0.0094 -0.0487 96  HIS B CA  
3033 C  C   . HIS B 96  ? 0.0299 0.0970 0.1061 -0.0447 0.0105  -0.0431 96  HIS B C   
3034 O  O   . HIS B 96  ? 0.0324 0.0976 0.1186 -0.0480 0.0162  -0.0465 96  HIS B O   
3035 C  CB  . HIS B 96  ? 0.0651 0.1023 0.1055 -0.0700 0.0125  -0.0498 96  HIS B CB  
3036 C  CG  . HIS B 96  ? 0.0339 0.1118 0.1168 -0.0504 0.0145  -0.0635 96  HIS B CG  
3037 N  ND1 . HIS B 96  ? 0.0360 0.1032 0.1280 -0.0518 0.0129  -0.0493 96  HIS B ND1 
3038 C  CD2 . HIS B 96  ? 0.0520 0.0913 0.1188 -0.0521 0.0039  -0.0579 96  HIS B CD2 
3039 C  CE1 . HIS B 96  ? 0.0221 0.1001 0.1046 -0.0304 0.0253  -0.0339 96  HIS B CE1 
3040 N  NE2 . HIS B 96  ? 0.0244 0.0732 0.1088 -0.0314 0.0110  -0.0533 96  HIS B NE2 
3041 N  N   . TRP B 97  ? 0.0413 0.0960 0.1174 -0.0552 0.0234  -0.0520 97  TRP B N   
3042 C  CA  . TRP B 97  ? 0.0340 0.0893 0.1373 -0.0472 0.0152  -0.0430 97  TRP B CA  
3043 C  C   . TRP B 97  ? 0.0337 0.0908 0.1131 -0.0468 0.0189  -0.0527 97  TRP B C   
3044 O  O   . TRP B 97  ? 0.0300 0.1130 0.1325 -0.0493 0.0152  -0.0521 97  TRP B O   
3045 C  CB  . TRP B 97  ? 0.0660 0.0839 0.1177 -0.0581 0.0101  -0.0576 97  TRP B CB  
3046 C  CG  . TRP B 97  ? 0.0712 0.0960 0.1140 -0.0669 0.0060  -0.0532 97  TRP B CG  
3047 C  CD1 . TRP B 97  ? 0.0784 0.1119 0.1284 -0.0532 0.0181  -0.0395 97  TRP B CD1 
3048 C  CD2 . TRP B 97  ? 0.0856 0.1054 0.1131 -0.0620 0.0118  -0.0402 97  TRP B CD2 
3049 N  NE1 . TRP B 97  ? 0.1202 0.1181 0.1387 -0.0785 0.0365  -0.0491 97  TRP B NE1 
3050 C  CE2 . TRP B 97  ? 0.0575 0.1272 0.1152 -0.0650 0.0134  -0.0400 97  TRP B CE2 
3051 C  CE3 . TRP B 97  ? 0.0671 0.1082 0.1247 -0.0668 -0.0094 -0.0473 97  TRP B CE3 
3052 C  CZ2 . TRP B 97  ? 0.1439 0.1236 0.1181 -0.0657 0.0038  -0.0510 97  TRP B CZ2 
3053 C  CZ3 . TRP B 97  ? 0.0755 0.1229 0.1342 -0.0777 -0.0170 -0.0407 97  TRP B CZ3 
3054 C  CH2 . TRP B 97  ? 0.1491 0.1161 0.1311 -0.0621 -0.0059 -0.0318 97  TRP B CH2 
3055 N  N   . GLY B 98  ? 0.0465 0.0760 0.1289 -0.0490 0.0190  -0.0568 98  GLY B N   
3056 C  CA  . GLY B 98  ? 0.0361 0.1103 0.1659 -0.0552 0.0410  -0.0649 98  GLY B CA  
3057 C  C   . GLY B 98  ? 0.0416 0.1046 0.1304 -0.0446 0.0094  -0.0478 98  GLY B C   
3058 O  O   . GLY B 98  ? 0.0613 0.1082 0.1294 -0.0521 0.0137  -0.0561 98  GLY B O   
3059 N  N   . SER B 99  ? 0.0493 0.1102 0.1403 -0.0433 0.0333  -0.0589 99  SER B N   
3060 C  CA  . SER B 99  ? 0.0575 0.1179 0.1494 -0.0479 0.0306  -0.0721 99  SER B CA  
3061 C  C   . SER B 99  ? 0.0411 0.1168 0.1627 -0.0473 0.0251  -0.0845 99  SER B C   
3062 O  O   . SER B 99  ? 0.0823 0.1522 0.1707 -0.0614 0.0212  -0.0906 99  SER B O   
3063 C  CB  . SER B 99  ? 0.0469 0.1286 0.1795 -0.0630 0.0478  -0.0696 99  SER B CB  
3064 O  OG  . SER B 99  ? 0.0651 0.1326 0.2050 -0.0356 0.0315  -0.0634 99  SER B OG  
3065 N  N   . LEU B 100 ? 0.0498 0.1254 0.1642 -0.0425 0.0272  -0.0427 100 LEU B N   
3066 C  CA  . LEU B 100 ? 0.0581 0.1304 0.2062 -0.0347 0.0425  -0.0370 100 LEU B CA  
3067 C  C   . LEU B 100 ? 0.0597 0.0746 0.1873 -0.0540 0.0380  -0.0381 100 LEU B C   
3068 O  O   . LEU B 100 ? 0.0857 0.0917 0.1870 -0.0580 0.0298  -0.0567 100 LEU B O   
3069 C  CB  . LEU B 100 ? 0.0913 0.1895 0.2861 -0.0001 0.0692  0.0167  100 LEU B CB  
3070 C  CG  . LEU B 100 ? 0.0784 0.2214 0.2952 -0.0131 0.0344  -0.0573 100 LEU B CG  
3071 C  CD1 . LEU B 100 ? 0.1188 0.2868 0.3641 -0.0097 0.0300  -0.0291 100 LEU B CD1 
3072 C  CD2 . LEU B 100 ? 0.2283 0.1814 0.3389 -0.1051 0.1122  -0.1119 100 LEU B CD2 
3073 N  N   . ASP B 101 ? 0.0336 0.1051 0.1738 -0.0484 0.0001  -0.0429 101 ASP B N   
3074 C  CA  . ASP B 101 ? 0.0462 0.1351 0.1847 -0.0469 0.0231  -0.0172 101 ASP B CA  
3075 C  C   . ASP B 101 ? 0.0268 0.1258 0.1931 -0.0491 0.0194  -0.0352 101 ASP B C   
3076 O  O   . ASP B 101 ? 0.1262 0.1170 0.2113 -0.0077 0.0414  -0.0280 101 ASP B O   
3077 C  CB  . ASP B 101 ? 0.0685 0.1351 0.1967 -0.0518 0.0018  -0.0373 101 ASP B CB  
3078 C  CG  . ASP B 101 ? 0.0480 0.2085 0.2303 -0.0915 0.0047  -0.0242 101 ASP B CG  
3079 O  OD1 . ASP B 101 ? 0.1114 0.1496 0.2247 -0.0611 -0.0013 -0.0351 101 ASP B OD1 
3080 O  OD2 . ASP B 101 ? 0.1810 0.2684 0.2861 -0.1852 -0.0669 0.0118  101 ASP B OD2 
3081 N  N   . GLY B 102 ? 0.0707 0.0879 0.2121 -0.0560 -0.0130 -0.0412 102 GLY B N   
3082 C  CA  . GLY B 102 ? 0.0426 0.1543 0.2055 -0.0726 -0.0010 -0.0199 102 GLY B CA  
3083 C  C   . GLY B 102 ? 0.0381 0.1213 0.1744 -0.0603 0.0147  -0.0221 102 GLY B C   
3084 O  O   . GLY B 102 ? 0.0727 0.1433 0.1651 -0.0432 0.0067  -0.0318 102 GLY B O   
3085 N  N   A GLN B 103 ? 0.0287 0.0870 0.1444 -0.0268 0.0523  -0.0506 103 GLN B N   
3086 N  N   B GLN B 103 ? 0.0779 0.1194 0.1716 -0.0578 0.0151  -0.0299 103 GLN B N   
3087 C  CA  A GLN B 103 ? 0.0230 0.1100 0.1491 -0.0392 0.0316  -0.0477 103 GLN B CA  
3088 C  CA  B GLN B 103 ? 0.0257 0.1381 0.1715 -0.0473 0.0195  -0.0357 103 GLN B CA  
3089 C  C   A GLN B 103 ? 0.0324 0.1131 0.1156 -0.0489 0.0403  -0.0485 103 GLN B C   
3090 C  C   B GLN B 103 ? 0.0458 0.1112 0.1399 -0.0486 0.0476  -0.0469 103 GLN B C   
3091 O  O   A GLN B 103 ? 0.0281 0.0886 0.1059 -0.0411 0.0391  -0.0626 103 GLN B O   
3092 O  O   B GLN B 103 ? 0.1278 0.1530 0.1685 -0.0813 -0.0190 -0.0525 103 GLN B O   
3093 C  CB  A GLN B 103 ? 0.0248 0.1411 0.1581 -0.0238 0.0510  -0.0307 103 GLN B CB  
3094 C  CB  B GLN B 103 ? 0.0339 0.1694 0.1785 -0.0244 0.0372  -0.0321 103 GLN B CB  
3095 C  CG  A GLN B 103 ? 0.0500 0.0766 0.1773 -0.0526 0.0636  -0.0534 103 GLN B CG  
3096 C  CG  B GLN B 103 ? 0.1227 0.1432 0.1997 0.0111  0.0582  -0.0392 103 GLN B CG  
3097 C  CD  A GLN B 103 ? 0.0875 0.1729 0.1827 0.0141  0.1070  0.0005  103 GLN B CD  
3098 C  CD  B GLN B 103 ? 0.1378 0.2342 0.2855 0.0425  0.0932  0.0264  103 GLN B CD  
3099 O  OE1 A GLN B 103 ? 0.0450 0.1538 0.3470 -0.0258 0.1024  0.0262  103 GLN B OE1 
3100 O  OE1 B GLN B 103 ? 0.1364 0.2989 0.3163 0.0105  0.1259  0.0666  103 GLN B OE1 
3101 N  NE2 A GLN B 103 ? 0.0148 0.2161 0.2048 0.0160  0.0366  -0.0147 103 GLN B NE2 
3102 N  NE2 B GLN B 103 ? 0.1425 0.2478 0.2155 0.0161  0.0485  -0.0328 103 GLN B NE2 
3103 N  N   . GLY B 104 ? 0.0141 0.1107 0.1532 -0.0279 0.0212  -0.0583 104 GLY B N   
3104 C  CA  . GLY B 104 ? 0.0218 0.1127 0.1360 -0.0397 0.0117  -0.0529 104 GLY B CA  
3105 C  C   . GLY B 104 ? 0.0182 0.1073 0.1149 -0.0346 0.0141  -0.0412 104 GLY B C   
3106 O  O   . GLY B 104 ? 0.0229 0.1091 0.1500 -0.0409 0.0211  -0.0380 104 GLY B O   
3107 N  N   . SER B 105 ? 0.0258 0.1187 0.1185 -0.0464 0.0180  -0.0552 105 SER B N   
3108 C  CA  . SER B 105 ? 0.0262 0.1225 0.1207 -0.0480 0.0225  -0.0558 105 SER B CA  
3109 C  C   . SER B 105 ? 0.0179 0.0983 0.1141 -0.0323 0.0135  -0.0504 105 SER B C   
3110 O  O   . SER B 105 ? 0.0168 0.1058 0.1272 -0.0304 0.0072  -0.0578 105 SER B O   
3111 C  CB  . SER B 105 ? 0.0315 0.1312 0.1387 -0.0554 0.0262  -0.0402 105 SER B CB  
3112 O  OG  . SER B 105 ? 0.0242 0.1007 0.1457 -0.0410 0.0192  -0.0464 105 SER B OG  
3113 N  N   . GLU B 106 ? 0.0254 0.0976 0.1107 -0.0402 0.0143  -0.0557 106 GLU B N   
3114 C  CA  . GLU B 106 ? 0.0236 0.1082 0.1182 -0.0389 0.0039  -0.0481 106 GLU B CA  
3115 C  C   . GLU B 106 ? 0.0256 0.0763 0.1191 -0.0366 0.0242  -0.0378 106 GLU B C   
3116 O  O   . GLU B 106 ? 0.0214 0.1152 0.1158 -0.0405 0.0190  -0.0433 106 GLU B O   
3117 C  CB  . GLU B 106 ? 0.0260 0.0996 0.1121 -0.0428 0.0193  -0.0409 106 GLU B CB  
3118 C  CG  . GLU B 106 ? 0.0617 0.0850 0.1224 -0.0522 0.0272  -0.0469 106 GLU B CG  
3119 C  CD  . GLU B 106 ? 0.0270 0.1173 0.1301 -0.0478 0.0279  -0.0705 106 GLU B CD  
3120 O  OE1 . GLU B 106 ? 0.0332 0.1023 0.1380 -0.0502 0.0275  -0.0647 106 GLU B OE1 
3121 O  OE2 . GLU B 106 ? 0.0172 0.1229 0.1492 -0.0346 0.0256  -0.0595 106 GLU B OE2 
3122 N  N   . HIS B 107 ? 0.0263 0.0906 0.1208 -0.0399 0.0157  -0.0537 107 HIS B N   
3123 C  CA  . HIS B 107 ? 0.0163 0.0851 0.1155 -0.0274 0.0216  -0.0447 107 HIS B CA  
3124 C  C   . HIS B 107 ? 0.0138 0.0936 0.1300 -0.0255 0.0162  -0.0557 107 HIS B C   
3125 O  O   . HIS B 107 ? 0.0157 0.0998 0.1224 -0.0292 0.0104  -0.0475 107 HIS B O   
3126 C  CB  . HIS B 107 ? 0.0126 0.0991 0.1474 -0.0231 0.0067  -0.0554 107 HIS B CB  
3127 C  CG  . HIS B 107 ? 0.0108 0.0973 0.1259 -0.0197 0.0090  -0.0586 107 HIS B CG  
3128 N  ND1 . HIS B 107 ? 0.0097 0.0920 0.1236 -0.0168 0.0070  -0.0500 107 HIS B ND1 
3129 C  CD2 . HIS B 107 ? 0.0097 0.0958 0.1352 -0.0162 0.0052  -0.0618 107 HIS B CD2 
3130 C  CE1 . HIS B 107 ? 0.0087 0.0936 0.1297 -0.0136 0.0016  -0.0436 107 HIS B CE1 
3131 N  NE2 . HIS B 107 ? 0.0106 0.1062 0.1144 -0.0206 0.0115  -0.0475 107 HIS B NE2 
3132 N  N   . THR B 108 ? 0.0192 0.0922 0.1434 -0.0326 0.0128  -0.0518 108 THR B N   
3133 C  CA  . THR B 108 ? 0.0133 0.0953 0.1259 -0.0249 0.0154  -0.0534 108 THR B CA  
3134 C  C   . THR B 108 ? 0.0142 0.0966 0.1154 -0.0259 0.0079  -0.0480 108 THR B C   
3135 O  O   . THR B 108 ? 0.0161 0.0976 0.1401 -0.0298 0.0133  -0.0506 108 THR B O   
3136 C  CB  . THR B 108 ? 0.0120 0.1171 0.1332 -0.0247 0.0065  -0.0489 108 THR B CB  
3137 O  OG1 . THR B 108 ? 0.0217 0.1254 0.1307 -0.0190 -0.0052 -0.0472 108 THR B OG1 
3138 C  CG2 . THR B 108 ? 0.0306 0.1003 0.1229 -0.0322 0.0149  -0.0605 108 THR B CG2 
3139 N  N   . VAL B 109 ? 0.0290 0.1111 0.1311 -0.0458 0.0114  -0.0372 109 VAL B N   
3140 C  CA  . VAL B 109 ? 0.0389 0.1146 0.1319 -0.0300 0.0243  -0.0274 109 VAL B CA  
3141 C  C   . VAL B 109 ? 0.0213 0.1145 0.1429 -0.0159 0.0257  -0.0323 109 VAL B C   
3142 O  O   . VAL B 109 ? 0.0437 0.1069 0.1663 -0.0226 0.0275  -0.0302 109 VAL B O   
3143 C  CB  . VAL B 109 ? 0.0194 0.1549 0.1896 -0.0344 0.0229  -0.0113 109 VAL B CB  
3144 C  CG1 . VAL B 109 ? 0.0615 0.1502 0.1995 -0.0565 0.0564  -0.0460 109 VAL B CG1 
3145 C  CG2 . VAL B 109 ? 0.0703 0.1414 0.1817 -0.0424 -0.0154 -0.0218 109 VAL B CG2 
3146 N  N   A ASP B 110 ? 0.0184 0.1504 0.1361 -0.0135 0.0369  0.0041  110 ASP B N   
3147 N  N   B ASP B 110 ? 0.0315 0.1256 0.1651 -0.0538 0.0038  -0.0300 110 ASP B N   
3148 C  CA  A ASP B 110 ? 0.0623 0.1307 0.1451 -0.0114 0.0292  -0.0148 110 ASP B CA  
3149 C  CA  B ASP B 110 ? 0.1084 0.1496 0.1818 -0.0131 0.0275  -0.0226 110 ASP B CA  
3150 C  C   A ASP B 110 ? 0.1049 0.1152 0.1632 0.0051  0.0331  -0.0198 110 ASP B C   
3151 C  C   B ASP B 110 ? 0.1202 0.1652 0.1828 -0.0211 0.0432  -0.0205 110 ASP B C   
3152 O  O   A ASP B 110 ? 0.0811 0.1122 0.1285 0.0026  0.0231  -0.0059 110 ASP B O   
3153 O  O   B ASP B 110 ? 0.1557 0.1623 0.1722 -0.0111 -0.0023 -0.0201 110 ASP B O   
3154 C  CB  A ASP B 110 ? 0.0924 0.1485 0.1594 -0.0171 0.0724  -0.0134 110 ASP B CB  
3155 C  CB  B ASP B 110 ? 0.1627 0.1532 0.2068 -0.0230 0.0688  -0.0089 110 ASP B CB  
3156 C  CG  A ASP B 110 ? 0.0709 0.1249 0.1139 -0.0414 0.0440  -0.0153 110 ASP B CG  
3157 C  CG  B ASP B 110 ? 0.1577 0.1793 0.2386 -0.0078 0.0533  -0.0337 110 ASP B CG  
3158 O  OD1 A ASP B 110 ? 0.0676 0.1449 0.1443 -0.0469 0.0341  -0.0369 110 ASP B OD1 
3159 O  OD1 B ASP B 110 ? 0.1693 0.1737 0.2694 -0.0290 0.0633  0.0000  110 ASP B OD1 
3160 O  OD2 A ASP B 110 ? 0.0653 0.1505 0.1710 -0.0432 0.0401  -0.0258 110 ASP B OD2 
3161 O  OD2 B ASP B 110 ? 0.1453 0.1623 0.2746 0.0228  0.0587  -0.0661 110 ASP B OD2 
3162 N  N   . LYS B 111 ? 0.0571 0.1364 0.1477 -0.0073 0.0044  -0.0185 111 LYS B N   
3163 C  CA  . LYS B 111 ? 0.0462 0.1300 0.1974 -0.0268 0.0074  -0.0369 111 LYS B CA  
3164 C  C   . LYS B 111 ? 0.0693 0.1393 0.1419 -0.0214 0.0201  -0.0122 111 LYS B C   
3165 O  O   . LYS B 111 ? 0.0284 0.1712 0.1870 -0.0147 0.0080  -0.0391 111 LYS B O   
3166 C  CB  . LYS B 111 ? 0.1177 0.1455 0.1782 0.0121  0.0352  -0.0231 111 LYS B CB  
3167 C  CG  . LYS B 111 ? 0.1329 0.2422 0.1848 0.0456  -0.0008 -0.0113 111 LYS B CG  
3168 C  CD  . LYS B 111 ? 0.1760 0.2877 0.2762 -0.0372 -0.0680 -0.0730 111 LYS B CD  
3169 C  CE  . LYS B 111 ? 0.2371 0.3242 0.2630 0.0001  -0.1085 -0.0406 111 LYS B CE  
3170 N  NZ  . LYS B 111 ? 0.1411 0.4542 0.3903 -0.0192 0.0608  0.0552  111 LYS B NZ  
3171 N  N   . LYS B 112 ? 0.0606 0.1218 0.1390 -0.0286 0.0192  -0.0181 112 LYS B N   
3172 C  CA  . LYS B 112 ? 0.0766 0.1421 0.1415 -0.0381 0.0334  -0.0336 112 LYS B CA  
3173 C  C   . LYS B 112 ? 0.0195 0.1195 0.1570 -0.0350 0.0255  -0.0352 112 LYS B C   
3174 O  O   . LYS B 112 ? 0.0214 0.1129 0.1457 -0.0372 0.0247  -0.0363 112 LYS B O   
3175 C  CB  . LYS B 112 ? 0.0811 0.1344 0.1771 -0.0664 0.0424  -0.0421 112 LYS B CB  
3176 C  CG  . LYS B 112 ? 0.1001 0.2057 0.1689 -0.0433 0.0190  -0.0533 112 LYS B CG  
3177 C  CD  . LYS B 112 ? 0.0985 0.2137 0.2257 -0.0798 0.0212  -0.0589 112 LYS B CD  
3178 C  CE  . LYS B 112 ? 0.1050 0.2670 0.2154 -0.0333 0.0066  -0.0201 112 LYS B CE  
3179 N  NZ  . LYS B 112 ? 0.2233 0.2437 0.2951 -0.0383 -0.0209 -0.0053 112 LYS B NZ  
3180 N  N   A LYS B 113 ? 0.0200 0.1261 0.1486 -0.0219 0.0122  -0.0487 113 LYS B N   
3181 N  N   B LYS B 113 ? 0.0295 0.1246 0.1529 -0.0065 0.0179  -0.0421 113 LYS B N   
3182 C  CA  A LYS B 113 ? 0.0204 0.1254 0.1467 -0.0182 0.0080  -0.0488 113 LYS B CA  
3183 C  CA  B LYS B 113 ? 0.0131 0.1301 0.1491 -0.0285 0.0068  -0.0488 113 LYS B CA  
3184 C  C   A LYS B 113 ? 0.0326 0.1106 0.1600 -0.0433 0.0062  -0.0386 113 LYS B C   
3185 C  C   B LYS B 113 ? 0.0275 0.1136 0.1650 -0.0452 0.0002  -0.0410 113 LYS B C   
3186 O  O   A LYS B 113 ? 0.0913 0.1055 0.2244 -0.0389 -0.0188 -0.0458 113 LYS B O   
3187 O  O   B LYS B 113 ? 0.0541 0.1181 0.2192 -0.0410 -0.0331 -0.0699 113 LYS B O   
3188 C  CB  A LYS B 113 ? 0.0272 0.1465 0.1426 -0.0129 0.0168  -0.0343 113 LYS B CB  
3189 C  CB  B LYS B 113 ? 0.0165 0.1524 0.1539 -0.0264 0.0237  -0.0283 113 LYS B CB  
3190 C  CG  A LYS B 113 ? 0.0164 0.1574 0.1890 0.0021  0.0091  -0.0658 113 LYS B CG  
3191 C  CG  B LYS B 113 ? 0.0264 0.1439 0.2153 -0.0519 0.0143  -0.0629 113 LYS B CG  
3192 C  CD  A LYS B 113 ? 0.0132 0.2148 0.1928 0.0122  0.0061  -0.0718 113 LYS B CD  
3193 C  CD  B LYS B 113 ? 0.0116 0.2175 0.2090 -0.0146 -0.0135 -0.0666 113 LYS B CD  
3194 C  CE  A LYS B 113 ? 0.0072 0.2984 0.2688 -0.0157 0.0064  -0.0498 113 LYS B CE  
3195 C  CE  B LYS B 113 ? 0.0170 0.2794 0.2566 -0.0132 -0.0392 -0.0814 113 LYS B CE  
3196 N  NZ  A LYS B 113 ? 0.0419 0.2425 0.3289 -0.0575 0.0943  -0.0507 113 LYS B NZ  
3197 N  NZ  B LYS B 113 ? 0.0929 0.2181 0.2876 -0.0228 -0.1018 -0.0966 113 LYS B NZ  
3198 N  N   . TYR B 114 ? 0.0212 0.1131 0.1388 -0.0388 0.0032  -0.0350 114 TYR B N   
3199 C  CA  . TYR B 114 ? 0.0280 0.0949 0.1463 -0.0408 0.0015  -0.0429 114 TYR B CA  
3200 C  C   . TYR B 114 ? 0.0366 0.0904 0.1421 -0.0487 0.0080  -0.0406 114 TYR B C   
3201 O  O   . TYR B 114 ? 0.0299 0.1010 0.1586 -0.0468 0.0124  -0.0420 114 TYR B O   
3202 C  CB  . TYR B 114 ? 0.0263 0.1021 0.1624 -0.0435 0.0277  -0.0517 114 TYR B CB  
3203 C  CG  . TYR B 114 ? 0.0191 0.1120 0.1449 -0.0365 0.0121  -0.0467 114 TYR B CG  
3204 C  CD1 . TYR B 114 ? 0.0206 0.1370 0.1982 -0.0430 0.0124  -0.0272 114 TYR B CD1 
3205 C  CD2 . TYR B 114 ? 0.0386 0.0996 0.1617 -0.0467 0.0006  -0.0446 114 TYR B CD2 
3206 C  CE1 . TYR B 114 ? 0.0877 0.1801 0.2113 -0.0412 0.0580  -0.0271 114 TYR B CE1 
3207 C  CE2 . TYR B 114 ? 0.0956 0.1703 0.1753 -0.0194 0.0418  -0.0381 114 TYR B CE2 
3208 C  CZ  . TYR B 114 ? 0.1121 0.1768 0.2029 -0.0598 0.0567  -0.0217 114 TYR B CZ  
3209 O  OH  . TYR B 114 ? 0.1957 0.2728 0.2238 -0.0605 0.1024  -0.0147 114 TYR B OH  
3210 N  N   . ALA B 115 ? 0.0321 0.0896 0.1368 -0.0404 0.0043  -0.0572 115 ALA B N   
3211 C  CA  . ALA B 115 ? 0.0602 0.0708 0.1402 -0.0478 0.0044  -0.0581 115 ALA B CA  
3212 C  C   . ALA B 115 ? 0.0339 0.0866 0.1545 -0.0469 0.0176  -0.0380 115 ALA B C   
3213 O  O   . ALA B 115 ? 0.0281 0.1130 0.1571 -0.0465 0.0078  -0.0486 115 ALA B O   
3214 C  CB  . ALA B 115 ? 0.0535 0.1136 0.1412 -0.0463 -0.0035 -0.0643 115 ALA B CB  
3215 N  N   . ALA B 116 ? 0.0387 0.0908 0.1461 -0.0501 0.0103  -0.0466 116 ALA B N   
3216 C  CA  . ALA B 116 ? 0.0553 0.0775 0.1289 -0.0513 0.0079  -0.0540 116 ALA B CA  
3217 C  C   . ALA B 116 ? 0.0283 0.0870 0.1235 -0.0385 0.0039  -0.0463 116 ALA B C   
3218 O  O   . ALA B 116 ? 0.0203 0.1016 0.1304 -0.0342 0.0010  -0.0396 116 ALA B O   
3219 C  CB  . ALA B 116 ? 0.0318 0.0811 0.1287 -0.0364 0.0000  -0.0401 116 ALA B CB  
3220 N  N   . GLU B 117 ? 0.0253 0.0864 0.1328 -0.0374 0.0099  -0.0419 117 GLU B N   
3221 C  CA  . GLU B 117 ? 0.0281 0.0949 0.1292 -0.0398 0.0005  -0.0446 117 GLU B CA  
3222 C  C   . GLU B 117 ? 0.0199 0.1177 0.0939 -0.0320 -0.0009 -0.0535 117 GLU B C   
3223 O  O   . GLU B 117 ? 0.0345 0.1075 0.1365 -0.0260 0.0288  -0.0416 117 GLU B O   
3224 C  CB  . GLU B 117 ? 0.0192 0.1064 0.1198 -0.0339 0.0060  -0.0502 117 GLU B CB  
3225 C  CG  . GLU B 117 ? 0.0186 0.0960 0.1254 -0.0314 0.0015  -0.0379 117 GLU B CG  
3226 C  CD  . GLU B 117 ? 0.0317 0.0818 0.1271 -0.0432 0.0098  -0.0324 117 GLU B CD  
3227 O  OE1 . GLU B 117 ? 0.0235 0.1071 0.1234 -0.0414 0.0122  -0.0396 117 GLU B OE1 
3228 O  OE2 . GLU B 117 ? 0.0430 0.0903 0.1100 -0.0363 -0.0126 -0.0389 117 GLU B OE2 
3229 N  N   . LEU B 118 ? 0.0257 0.0856 0.1182 -0.0326 -0.0005 -0.0513 118 LEU B N   
3230 C  CA  . LEU B 118 ? 0.0401 0.0929 0.1168 -0.0405 -0.0110 -0.0486 118 LEU B CA  
3231 C  C   . LEU B 118 ? 0.0424 0.0839 0.1070 -0.0431 -0.0121 -0.0356 118 LEU B C   
3232 O  O   . LEU B 118 ? 0.0409 0.1068 0.1157 -0.0525 -0.0044 -0.0406 118 LEU B O   
3233 C  CB  . LEU B 118 ? 0.0393 0.1100 0.1318 -0.0407 -0.0225 -0.0416 118 LEU B CB  
3234 C  CG  . LEU B 118 ? 0.0362 0.1026 0.1368 -0.0380 -0.0190 -0.0484 118 LEU B CG  
3235 C  CD1 . LEU B 118 ? 0.0581 0.1295 0.1587 -0.0545 -0.0377 -0.0450 118 LEU B CD1 
3236 C  CD2 . LEU B 118 ? 0.0445 0.1385 0.1773 -0.0384 -0.0509 -0.0469 118 LEU B CD2 
3237 N  N   . HIS B 119 ? 0.0378 0.0892 0.1166 -0.0427 -0.0101 -0.0375 119 HIS B N   
3238 C  CA  . HIS B 119 ? 0.0420 0.0894 0.1098 -0.0478 -0.0077 -0.0336 119 HIS B CA  
3239 C  C   . HIS B 119 ? 0.0416 0.0966 0.1107 -0.0499 -0.0067 -0.0356 119 HIS B C   
3240 O  O   . HIS B 119 ? 0.0393 0.0947 0.1150 -0.0388 -0.0082 -0.0436 119 HIS B O   
3241 C  CB  . HIS B 119 ? 0.0240 0.1000 0.1235 -0.0362 -0.0023 -0.0426 119 HIS B CB  
3242 C  CG  . HIS B 119 ? 0.0196 0.0932 0.1069 -0.0304 0.0017  -0.0450 119 HIS B CG  
3243 N  ND1 . HIS B 119 ? 0.0250 0.1101 0.1306 -0.0411 0.0071  -0.0553 119 HIS B ND1 
3244 C  CD2 . HIS B 119 ? 0.0498 0.0820 0.1016 -0.0438 -0.0006 -0.0422 119 HIS B CD2 
3245 C  CE1 . HIS B 119 ? 0.0277 0.0838 0.1164 -0.0381 0.0273  -0.0751 119 HIS B CE1 
3246 N  NE2 . HIS B 119 ? 0.0146 0.0922 0.1079 -0.0261 0.0111  -0.0527 119 HIS B NE2 
3247 N  N   . LEU B 120 ? 0.0447 0.0811 0.1354 -0.0394 -0.0144 -0.0502 120 LEU B N   
3248 C  CA  . LEU B 120 ? 0.0345 0.1133 0.1672 -0.0421 -0.0247 -0.0414 120 LEU B CA  
3249 C  C   . LEU B 120 ? 0.0226 0.0871 0.1400 -0.0279 -0.0152 -0.0359 120 LEU B C   
3250 O  O   . LEU B 120 ? 0.0302 0.0972 0.1267 -0.0416 -0.0008 -0.0449 120 LEU B O   
3251 C  CB  . LEU B 120 ? 0.0476 0.1165 0.2080 -0.0481 -0.0381 -0.0500 120 LEU B CB  
3252 C  CG  . LEU B 120 ? 0.0705 0.1439 0.2399 -0.0686 -0.0664 -0.0321 120 LEU B CG  
3253 C  CD1 . LEU B 120 ? 0.1430 0.1456 0.2121 -0.0983 -0.0066 -0.0649 120 LEU B CD1 
3254 C  CD2 . LEU B 120 ? 0.1012 0.1386 0.2346 -0.0214 -0.0922 -0.0753 120 LEU B CD2 
3255 N  N   . VAL B 121 ? 0.0499 0.1010 0.1330 -0.0558 -0.0103 -0.0403 121 VAL B N   
3256 C  CA  . VAL B 121 ? 0.0673 0.0676 0.1414 -0.0512 -0.0055 -0.0445 121 VAL B CA  
3257 C  C   . VAL B 121 ? 0.0635 0.0849 0.1505 -0.0590 -0.0116 -0.0379 121 VAL B C   
3258 O  O   . VAL B 121 ? 0.1197 0.0879 0.1478 -0.0498 -0.0334 -0.0480 121 VAL B O   
3259 C  CB  . VAL B 121 ? 0.0762 0.1050 0.1453 -0.0414 0.0026  -0.0576 121 VAL B CB  
3260 C  CG1 . VAL B 121 ? 0.0940 0.1134 0.1499 -0.0580 0.0055  -0.0518 121 VAL B CG1 
3261 C  CG2 . VAL B 121 ? 0.0562 0.1107 0.1411 -0.0496 0.0051  -0.0461 121 VAL B CG2 
3262 N  N   . HIS B 122 ? 0.0484 0.0895 0.1480 -0.0424 -0.0178 -0.0557 122 HIS B N   
3263 C  CA  . HIS B 122 ? 0.0518 0.0937 0.1301 -0.0384 -0.0097 -0.0515 122 HIS B CA  
3264 C  C   . HIS B 122 ? 0.0386 0.1014 0.1326 -0.0403 -0.0082 -0.0471 122 HIS B C   
3265 O  O   . HIS B 122 ? 0.0556 0.0849 0.1565 -0.0506 -0.0198 -0.0412 122 HIS B O   
3266 C  CB  . HIS B 122 ? 0.0398 0.0854 0.1611 -0.0346 -0.0141 -0.0483 122 HIS B CB  
3267 C  CG  . HIS B 122 ? 0.0253 0.1140 0.1866 -0.0372 -0.0147 -0.0472 122 HIS B CG  
3268 N  ND1 . HIS B 122 ? 0.0292 0.1037 0.1806 -0.0398 -0.0154 -0.0403 122 HIS B ND1 
3269 C  CD2 . HIS B 122 ? 0.0370 0.1234 0.2112 -0.0519 -0.0152 -0.0496 122 HIS B CD2 
3270 C  CE1 . HIS B 122 ? 0.0238 0.0983 0.1911 -0.0350 -0.0054 -0.0531 122 HIS B CE1 
3271 N  NE2 . HIS B 122 ? 0.0437 0.1070 0.1893 -0.0447 -0.0252 -0.0580 122 HIS B NE2 
3272 N  N   . TRP B 123 ? 0.0376 0.0892 0.1625 -0.0442 -0.0031 -0.0514 123 TRP B N   
3273 C  CA  . TRP B 123 ? 0.0416 0.1026 0.1563 -0.0535 0.0046  -0.0548 123 TRP B CA  
3274 C  C   . TRP B 123 ? 0.0284 0.0974 0.1682 -0.0365 -0.0155 -0.0428 123 TRP B C   
3275 O  O   . TRP B 123 ? 0.0324 0.1131 0.1876 -0.0378 -0.0272 -0.0495 123 TRP B O   
3276 C  CB  . TRP B 123 ? 0.0696 0.1290 0.1508 -0.0719 0.0126  -0.0525 123 TRP B CB  
3277 C  CG  . TRP B 123 ? 0.1266 0.1276 0.1969 -0.0710 -0.0120 -0.0419 123 TRP B CG  
3278 C  CD1 . TRP B 123 ? 0.2663 0.1680 0.1895 -0.1339 -0.0314 -0.0431 123 TRP B CD1 
3279 C  CD2 . TRP B 123 ? 0.1717 0.1055 0.1729 -0.0979 -0.0083 -0.0290 123 TRP B CD2 
3280 N  NE1 . TRP B 123 ? 0.3146 0.1159 0.2143 -0.1216 -0.0713 -0.0719 123 TRP B NE1 
3281 C  CE2 . TRP B 123 ? 0.2189 0.0980 0.2006 -0.1028 -0.0584 -0.0416 123 TRP B CE2 
3282 C  CE3 . TRP B 123 ? 0.1473 0.1095 0.2012 -0.0875 -0.0272 -0.0409 123 TRP B CE3 
3283 C  CZ2 . TRP B 123 ? 0.2217 0.1195 0.2630 -0.0952 -0.0770 -0.0221 123 TRP B CZ2 
3284 C  CZ3 . TRP B 123 ? 0.1264 0.1170 0.2493 -0.1043 -0.0401 -0.0195 123 TRP B CZ3 
3285 C  CH2 . TRP B 123 ? 0.2333 0.1286 0.2385 -0.0834 -0.0436 -0.0104 123 TRP B CH2 
3286 N  N   . ASN B 124 ? 0.0317 0.1083 0.1680 -0.0348 -0.0199 -0.0612 124 ASN B N   
3287 C  CA  . ASN B 124 ? 0.0271 0.1193 0.1815 -0.0366 -0.0147 -0.0629 124 ASN B CA  
3288 C  C   . ASN B 124 ? 0.0266 0.1185 0.1699 -0.0433 0.0045  -0.0658 124 ASN B C   
3289 O  O   . ASN B 124 ? 0.0276 0.1267 0.1778 -0.0458 0.0019  -0.0648 124 ASN B O   
3290 C  CB  . ASN B 124 ? 0.0357 0.1247 0.1645 -0.0469 -0.0003 -0.0745 124 ASN B CB  
3291 C  CG  . ASN B 124 ? 0.0383 0.1028 0.1892 -0.0522 0.0133  -0.0615 124 ASN B CG  
3292 O  OD1 . ASN B 124 ? 0.0599 0.1354 0.2186 -0.0215 0.0192  -0.0666 124 ASN B OD1 
3293 N  ND2 . ASN B 124 ? 0.0922 0.1170 0.1597 -0.0362 0.0026  -0.0839 124 ASN B ND2 
3294 N  N   . THR B 125 ? 0.0331 0.0961 0.2044 -0.0272 -0.0091 -0.0709 125 THR B N   
3295 C  CA  . THR B 125 ? 0.1040 0.1140 0.2161 -0.0229 -0.0542 -0.0685 125 THR B CA  
3296 C  C   . THR B 125 ? 0.0485 0.1054 0.2548 -0.0421 -0.0362 -0.0619 125 THR B C   
3297 O  O   . THR B 125 ? 0.0839 0.1456 0.2911 -0.0336 -0.0199 -0.0350 125 THR B O   
3298 C  CB  . THR B 125 ? 0.1227 0.1600 0.2627 -0.0525 -0.0903 -0.0353 125 THR B CB  
3299 O  OG1 . THR B 125 ? 0.0839 0.2097 0.4013 0.0015  0.0215  -0.0366 125 THR B OG1 
3300 C  CG2 . THR B 125 ? 0.1415 0.1889 0.3084 -0.0795 -0.0946 -0.0605 125 THR B CG2 
3301 N  N   . LYS B 126 ? 0.0148 0.1416 0.2467 -0.0291 0.0007  -0.0941 126 LYS B N   
3302 C  CA  . LYS B 126 ? 0.1010 0.1256 0.2770 -0.0427 0.0122  -0.1085 126 LYS B CA  
3303 C  C   . LYS B 126 ? 0.0906 0.0936 0.2799 -0.0475 -0.0108 -0.0861 126 LYS B C   
3304 O  O   . LYS B 126 ? 0.0976 0.1271 0.3640 -0.0710 0.0066  -0.1342 126 LYS B O   
3305 C  CB  . LYS B 126 ? 0.1873 0.1512 0.3057 -0.0803 -0.0008 -0.1116 126 LYS B CB  
3306 C  CG  . LYS B 126 ? 0.1188 0.1895 0.3328 -0.0429 0.0394  -0.1094 126 LYS B CG  
3307 C  CD  . LYS B 126 ? 0.2773 0.2794 0.3353 -0.1126 0.0693  -0.0392 126 LYS B CD  
3308 C  CE  . LYS B 126 ? 0.3649 0.3893 0.6315 0.1516  -0.0337 -0.1423 126 LYS B CE  
3309 N  NZ  . LYS B 126 ? 0.3057 0.6662 0.5692 -0.0089 -0.0478 -0.3170 126 LYS B NZ  
3310 N  N   . TYR B 127 ? 0.0744 0.0863 0.2015 -0.0462 -0.0128 -0.0609 127 TYR B N   
3311 C  CA  . TYR B 127 ? 0.0653 0.1112 0.2109 -0.0493 -0.0275 -0.0671 127 TYR B CA  
3312 C  C   . TYR B 127 ? 0.0693 0.0897 0.2223 -0.0602 -0.0022 -0.0726 127 TYR B C   
3313 O  O   . TYR B 127 ? 0.0468 0.1275 0.2509 -0.0599 -0.0249 -0.0332 127 TYR B O   
3314 C  CB  . TYR B 127 ? 0.0482 0.1244 0.2391 -0.0395 -0.0059 -0.0419 127 TYR B CB  
3315 C  CG  . TYR B 127 ? 0.0737 0.1112 0.2056 -0.0423 -0.0119 -0.0757 127 TYR B CG  
3316 C  CD1 . TYR B 127 ? 0.0734 0.1442 0.2124 -0.0442 -0.0359 -0.0819 127 TYR B CD1 
3317 C  CD2 . TYR B 127 ? 0.0482 0.1154 0.2104 -0.0443 0.0085  -0.0469 127 TYR B CD2 
3318 C  CE1 . TYR B 127 ? 0.0899 0.1184 0.2172 -0.0465 -0.0218 -0.0936 127 TYR B CE1 
3319 C  CE2 . TYR B 127 ? 0.0317 0.1486 0.2050 -0.0545 0.0016  -0.0703 127 TYR B CE2 
3320 C  CZ  . TYR B 127 ? 0.1324 0.1289 0.2059 -0.0269 -0.0104 -0.0688 127 TYR B CZ  
3321 O  OH  . TYR B 127 ? 0.1364 0.1831 0.2108 -0.0128 -0.0262 -0.0665 127 TYR B OH  
3322 N  N   . GLY B 128 ? 0.0775 0.1344 0.2214 -0.0577 -0.0147 -0.0465 128 GLY B N   
3323 C  CA  . GLY B 128 ? 0.0930 0.1167 0.2426 -0.0632 -0.0145 -0.0273 128 GLY B CA  
3324 C  C   . GLY B 128 ? 0.1183 0.1033 0.2080 -0.0671 -0.0399 -0.0268 128 GLY B C   
3325 O  O   . GLY B 128 ? 0.1010 0.1448 0.2438 -0.0577 -0.0550 -0.0010 128 GLY B O   
3326 N  N   . ASP B 129 ? 0.0931 0.1130 0.2151 -0.0552 -0.0177 -0.0359 129 ASP B N   
3327 C  CA  . ASP B 129 ? 0.1394 0.1441 0.1892 -0.0604 -0.0139 -0.0390 129 ASP B CA  
3328 C  C   . ASP B 129 ? 0.0791 0.1318 0.1630 -0.0622 -0.0088 -0.0421 129 ASP B C   
3329 O  O   . ASP B 129 ? 0.0996 0.1159 0.1777 -0.0625 -0.0227 -0.0549 129 ASP B O   
3330 C  CB  . ASP B 129 ? 0.1138 0.1119 0.2034 -0.0643 -0.0111 -0.0436 129 ASP B CB  
3331 C  CG  . ASP B 129 ? 0.0739 0.1310 0.2465 -0.0344 0.0237  -0.0816 129 ASP B CG  
3332 O  OD1 . ASP B 129 ? 0.1498 0.1489 0.2963 -0.0523 -0.0325 -0.0266 129 ASP B OD1 
3333 O  OD2 . ASP B 129 ? 0.1268 0.1439 0.3796 -0.0461 -0.0272 -0.0546 129 ASP B OD2 
3334 N  N   . VAL B 130 ? 0.1309 0.1289 0.1558 -0.0483 -0.0146 -0.0441 130 VAL B N   
3335 C  CA  . VAL B 130 ? 0.1185 0.1254 0.1685 -0.0342 -0.0253 -0.0552 130 VAL B CA  
3336 C  C   . VAL B 130 ? 0.1033 0.1156 0.1459 -0.0502 -0.0069 -0.0529 130 VAL B C   
3337 O  O   . VAL B 130 ? 0.0773 0.1251 0.1450 -0.0458 0.0017  -0.0376 130 VAL B O   
3338 C  CB  . VAL B 130 ? 0.1263 0.1308 0.1738 -0.0594 -0.0438 -0.0572 130 VAL B CB  
3339 C  CG1 . VAL B 130 ? 0.1985 0.1958 0.1918 -0.0889 -0.0471 -0.0370 130 VAL B CG1 
3340 C  CG2 . VAL B 130 ? 0.2502 0.1559 0.1908 -0.0174 -0.0863 -0.0672 130 VAL B CG2 
3341 N  N   . GLY B 131 ? 0.1271 0.1525 0.1603 -0.0701 0.0164  -0.0378 131 GLY B N   
3342 C  CA  . GLY B 131 ? 0.1143 0.1934 0.1684 -0.0886 0.0137  -0.0524 131 GLY B CA  
3343 C  C   . GLY B 131 ? 0.0588 0.1536 0.1604 -0.0714 0.0171  -0.0397 131 GLY B C   
3344 O  O   . GLY B 131 ? 0.0785 0.1421 0.1881 -0.0615 0.0036  -0.0482 131 GLY B O   
3345 N  N   A LYS B 132 ? 0.0663 0.1331 0.1745 -0.0747 -0.0002 -0.0374 132 LYS B N   
3346 N  N   B LYS B 132 ? 0.0651 0.1353 0.1747 -0.0736 -0.0004 -0.0378 132 LYS B N   
3347 C  CA  A LYS B 132 ? 0.0573 0.1434 0.1796 -0.0670 0.0100  -0.0438 132 LYS B CA  
3348 C  CA  B LYS B 132 ? 0.0556 0.1419 0.1799 -0.0653 0.0122  -0.0433 132 LYS B CA  
3349 C  C   A LYS B 132 ? 0.0560 0.0936 0.1685 -0.0581 0.0038  -0.0603 132 LYS B C   
3350 C  C   B LYS B 132 ? 0.0561 0.0945 0.1681 -0.0582 0.0036  -0.0608 132 LYS B C   
3351 O  O   A LYS B 132 ? 0.0534 0.1391 0.1790 -0.0753 0.0027  -0.0501 132 LYS B O   
3352 O  O   B LYS B 132 ? 0.0524 0.1377 0.1780 -0.0742 0.0030  -0.0498 132 LYS B O   
3353 C  CB  A LYS B 132 ? 0.0608 0.1390 0.2003 -0.0653 0.0080  -0.0649 132 LYS B CB  
3354 C  CB  B LYS B 132 ? 0.0597 0.1429 0.1941 -0.0585 0.0062  -0.0603 132 LYS B CB  
3355 C  CG  A LYS B 132 ? 0.1392 0.1714 0.2506 -0.1005 -0.0340 -0.0320 132 LYS B CG  
3356 C  CG  B LYS B 132 ? 0.1658 0.1620 0.2908 -0.0875 -0.0321 -0.0221 132 LYS B CG  
3357 C  CD  A LYS B 132 ? 0.2027 0.2037 0.4796 -0.1268 -0.0205 -0.0359 132 LYS B CD  
3358 C  CD  B LYS B 132 ? 0.2252 0.2675 0.3404 -0.0245 -0.0150 -0.0438 132 LYS B CD  
3359 C  CE  A LYS B 132 ? 0.4193 0.2042 0.5416 -0.2376 -0.1626 -0.0012 132 LYS B CE  
3360 C  CE  B LYS B 132 ? 0.2592 0.2612 0.4425 0.1111  0.0528  0.0179  132 LYS B CE  
3361 N  NZ  A LYS B 132 ? 0.3380 0.4574 0.6036 -0.1866 -0.2184 0.0817  132 LYS B NZ  
3362 N  NZ  B LYS B 132 ? 0.3597 0.3943 0.5088 0.0905  0.0540  0.0103  132 LYS B NZ  
3363 N  N   . ALA B 133 ? 0.0540 0.0978 0.1529 -0.0599 0.0032  -0.0528 133 ALA B N   
3364 C  CA  . ALA B 133 ? 0.0515 0.1305 0.1154 -0.0480 -0.0091 -0.0502 133 ALA B CA  
3365 C  C   . ALA B 133 ? 0.0417 0.1375 0.1309 -0.0608 -0.0061 -0.0463 133 ALA B C   
3366 O  O   . ALA B 133 ? 0.0319 0.1352 0.1483 -0.0529 0.0005  -0.0532 133 ALA B O   
3367 C  CB  . ALA B 133 ? 0.0416 0.1088 0.1548 -0.0477 -0.0144 -0.0398 133 ALA B CB  
3368 N  N   . LEU B 134 ? 0.0500 0.1224 0.1461 -0.0650 0.0071  -0.0620 134 LEU B N   
3369 C  CA  . LEU B 134 ? 0.0455 0.1357 0.1434 -0.0633 0.0081  -0.0414 134 LEU B CA  
3370 C  C   . LEU B 134 ? 0.0191 0.1498 0.1724 -0.0420 0.0045  -0.0428 134 LEU B C   
3371 O  O   . LEU B 134 ? 0.0491 0.1441 0.1824 -0.0458 -0.0125 -0.0547 134 LEU B O   
3372 C  CB  . LEU B 134 ? 0.0560 0.1285 0.1672 -0.0614 0.0294  -0.0496 134 LEU B CB  
3373 C  CG  . LEU B 134 ? 0.1198 0.1349 0.1856 -0.0514 0.0269  -0.0790 134 LEU B CG  
3374 C  CD1 . LEU B 134 ? 0.2248 0.2041 0.2524 -0.0864 0.1120  -0.0861 134 LEU B CD1 
3375 C  CD2 . LEU B 134 ? 0.1788 0.1480 0.2019 -0.0917 0.0181  -0.0624 134 LEU B CD2 
3376 N  N   . GLN B 135 ? 0.0363 0.1470 0.1551 -0.0593 0.0013  -0.0618 135 GLN B N   
3377 C  CA  . GLN B 135 ? 0.0519 0.1627 0.1791 -0.0741 -0.0091 -0.0631 135 GLN B CA  
3378 C  C   . GLN B 135 ? 0.0374 0.1257 0.1768 -0.0497 -0.0214 -0.0441 135 GLN B C   
3379 O  O   . GLN B 135 ? 0.0462 0.1834 0.1890 -0.0741 0.0006  -0.0855 135 GLN B O   
3380 C  CB  . GLN B 135 ? 0.0909 0.2490 0.2460 -0.1387 0.0100  -0.0760 135 GLN B CB  
3381 C  CG  . GLN B 135 ? 0.1291 0.2219 0.2436 -0.1398 0.0008  -0.0568 135 GLN B CG  
3382 C  CD  . GLN B 135 ? 0.2458 0.2091 0.3917 -0.1604 -0.0034 -0.0563 135 GLN B CD  
3383 O  OE1 . GLN B 135 ? 0.2893 0.5187 0.5247 -0.2383 -0.1341 -0.0486 135 GLN B OE1 
3384 N  NE2 . GLN B 135 ? 0.2293 0.2597 0.4429 -0.1363 0.0637  -0.0362 135 GLN B NE2 
3385 N  N   . GLN B 136 ? 0.0348 0.1201 0.1583 -0.0491 -0.0093 -0.0491 136 GLN B N   
3386 C  CA  . GLN B 136 ? 0.0593 0.1180 0.1395 -0.0637 -0.0078 -0.0582 136 GLN B CA  
3387 C  C   . GLN B 136 ? 0.0237 0.1210 0.1572 -0.0445 0.0228  -0.0642 136 GLN B C   
3388 O  O   . GLN B 136 ? 0.0356 0.1132 0.1469 -0.0447 0.0033  -0.0593 136 GLN B O   
3389 C  CB  . GLN B 136 ? 0.0800 0.1283 0.1533 -0.0450 0.0005  -0.0497 136 GLN B CB  
3390 C  CG  . GLN B 136 ? 0.1331 0.1703 0.2176 -0.0606 -0.0034 -0.0283 136 GLN B CG  
3391 C  CD  . GLN B 136 ? 0.0673 0.1908 0.2863 -0.0716 0.0194  -0.0227 136 GLN B CD  
3392 O  OE1 . GLN B 136 ? 0.1992 0.2304 0.3019 -0.0284 -0.0810 -0.1738 136 GLN B OE1 
3393 N  NE2 . GLN B 136 ? 0.1905 0.2568 0.2655 -0.0969 0.0526  -0.0048 136 GLN B NE2 
3394 N  N   . PRO B 137 ? 0.0327 0.1312 0.1588 -0.0532 0.0010  -0.0533 137 PRO B N   
3395 C  CA  . PRO B 137 ? 0.0150 0.1327 0.1365 -0.0325 0.0078  -0.0535 137 PRO B CA  
3396 C  C   . PRO B 137 ? 0.0250 0.1337 0.1527 -0.0483 0.0088  -0.0403 137 PRO B C   
3397 O  O   . PRO B 137 ? 0.0619 0.1426 0.2386 -0.0381 -0.0052 -0.0304 137 PRO B O   
3398 C  CB  . PRO B 137 ? 0.0430 0.1990 0.1418 -0.0414 -0.0011 -0.0560 137 PRO B CB  
3399 C  CG  . PRO B 137 ? 0.1703 0.1987 0.1915 -0.0536 0.0187  -0.0515 137 PRO B CG  
3400 C  CD  . PRO B 137 ? 0.0976 0.1578 0.1624 -0.0652 0.0065  -0.0816 137 PRO B CD  
3401 N  N   . ASP B 138 ? 0.0316 0.1207 0.1631 -0.0511 0.0055  -0.0521 138 ASP B N   
3402 C  CA  . ASP B 138 ? 0.0330 0.1633 0.1490 -0.0646 0.0188  -0.0415 138 ASP B CA  
3403 C  C   . ASP B 138 ? 0.0244 0.1045 0.1490 -0.0417 0.0199  -0.0447 138 ASP B C   
3404 O  O   . ASP B 138 ? 0.0280 0.1638 0.1749 -0.0172 0.0047  -0.0489 138 ASP B O   
3405 C  CB  . ASP B 138 ? 0.0488 0.1759 0.1544 -0.0421 0.0225  -0.0306 138 ASP B CB  
3406 C  CG  . ASP B 138 ? 0.0275 0.1710 0.1916 -0.0293 0.0189  -0.0566 138 ASP B CG  
3407 O  OD1 . ASP B 138 ? 0.0753 0.1590 0.1767 -0.0286 0.0239  -0.0514 138 ASP B OD1 
3408 O  OD2 . ASP B 138 ? 0.1321 0.2195 0.2163 0.0203  0.0280  -0.0862 138 ASP B OD2 
3409 N  N   . GLY B 139 ? 0.0243 0.1120 0.1529 -0.0422 0.0124  -0.0587 139 GLY B N   
3410 C  CA  . GLY B 139 ? 0.0324 0.0985 0.1575 -0.0447 -0.0004 -0.0475 139 GLY B CA  
3411 C  C   . GLY B 139 ? 0.0148 0.0945 0.1253 -0.0272 0.0144  -0.0539 139 GLY B C   
3412 O  O   . GLY B 139 ? 0.0301 0.1003 0.1502 -0.0410 -0.0094 -0.0408 139 GLY B O   
3413 N  N   . LEU B 140 ? 0.0195 0.1014 0.1455 -0.0333 0.0103  -0.0629 140 LEU B N   
3414 C  CA  . LEU B 140 ? 0.0261 0.1025 0.1353 -0.0432 0.0240  -0.0650 140 LEU B CA  
3415 C  C   . LEU B 140 ? 0.0206 0.1037 0.1424 -0.0360 0.0107  -0.0556 140 LEU B C   
3416 O  O   . LEU B 140 ? 0.0199 0.1041 0.1331 -0.0363 0.0191  -0.0480 140 LEU B O   
3417 C  CB  . LEU B 140 ? 0.0190 0.1122 0.1471 -0.0356 0.0147  -0.0669 140 LEU B CB  
3418 C  CG  . LEU B 140 ? 0.0459 0.1547 0.1717 -0.0225 0.0487  -0.0568 140 LEU B CG  
3419 C  CD1 . LEU B 140 ? 0.1515 0.1562 0.2735 -0.0178 0.0509  -0.0269 140 LEU B CD1 
3420 C  CD2 . LEU B 140 ? 0.0356 0.1794 0.2007 -0.0260 0.0498  -0.0566 140 LEU B CD2 
3421 N  N   . ALA B 141 ? 0.0345 0.1000 0.1599 -0.0455 -0.0068 -0.0444 141 ALA B N   
3422 C  CA  . ALA B 141 ? 0.0267 0.1025 0.1774 -0.0435 0.0182  -0.0609 141 ALA B CA  
3423 C  C   . ALA B 141 ? 0.0185 0.1036 0.1291 -0.0338 0.0074  -0.0392 141 ALA B C   
3424 O  O   . ALA B 141 ? 0.0417 0.1024 0.1499 -0.0541 -0.0055 -0.0344 141 ALA B O   
3425 C  CB  . ALA B 141 ? 0.0202 0.1502 0.1789 -0.0425 0.0301  -0.0547 141 ALA B CB  
3426 N  N   . VAL B 142 ? 0.0137 0.1037 0.1321 -0.0258 0.0062  -0.0501 142 VAL B N   
3427 C  CA  . VAL B 142 ? 0.0254 0.1115 0.1592 -0.0447 0.0215  -0.0564 142 VAL B CA  
3428 C  C   . VAL B 142 ? 0.0333 0.1196 0.1515 -0.0516 0.0019  -0.0492 142 VAL B C   
3429 O  O   . VAL B 142 ? 0.0254 0.1126 0.1459 -0.0427 0.0050  -0.0495 142 VAL B O   
3430 C  CB  . VAL B 142 ? 0.0175 0.1274 0.1375 -0.0367 0.0163  -0.0556 142 VAL B CB  
3431 C  CG1 . VAL B 142 ? 0.0345 0.1176 0.1253 -0.0278 -0.0023 -0.0542 142 VAL B CG1 
3432 C  CG2 . VAL B 142 ? 0.0286 0.1522 0.1725 -0.0564 0.0127  -0.0536 142 VAL B CG2 
3433 N  N   . LEU B 143 ? 0.0384 0.1116 0.1790 -0.0500 0.0001  -0.0688 143 LEU B N   
3434 C  CA  . LEU B 143 ? 0.0231 0.1436 0.2159 -0.0403 -0.0182 -0.0438 143 LEU B CA  
3435 C  C   . LEU B 143 ? 0.0303 0.1622 0.1429 -0.0553 -0.0081 -0.0420 143 LEU B C   
3436 O  O   . LEU B 143 ? 0.0295 0.1104 0.1496 -0.0420 -0.0126 -0.0388 143 LEU B O   
3437 C  CB  . LEU B 143 ? 0.0386 0.1627 0.2698 -0.0431 -0.0536 -0.0596 143 LEU B CB  
3438 C  CG  . LEU B 143 ? 0.0576 0.2675 0.4103 -0.0471 -0.1262 -0.0260 143 LEU B CG  
3439 C  CD1 . LEU B 143 ? 0.0353 0.2635 0.3750 -0.0727 -0.0336 -0.0719 143 LEU B CD1 
3440 C  CD2 . LEU B 143 ? 0.0635 0.4874 0.6008 -0.0786 -0.1553 -0.0396 143 LEU B CD2 
3441 N  N   . GLY B 144 ? 0.0204 0.1220 0.1606 -0.0357 -0.0008 -0.0597 144 GLY B N   
3442 C  CA  . GLY B 144 ? 0.0208 0.1100 0.1297 -0.0362 0.0032  -0.0482 144 GLY B CA  
3443 C  C   . GLY B 144 ? 0.0244 0.0881 0.1149 -0.0351 0.0018  -0.0415 144 GLY B C   
3444 O  O   . GLY B 144 ? 0.0357 0.1085 0.1142 -0.0494 0.0055  -0.0345 144 GLY B O   
3445 N  N   . ILE B 145 ? 0.0225 0.0969 0.1360 -0.0326 0.0003  -0.0571 145 ILE B N   
3446 C  CA  . ILE B 145 ? 0.0290 0.1105 0.1419 -0.0387 -0.0136 -0.0468 145 ILE B CA  
3447 C  C   . ILE B 145 ? 0.0177 0.1134 0.1229 -0.0253 -0.0154 -0.0356 145 ILE B C   
3448 O  O   . ILE B 145 ? 0.0339 0.0975 0.1327 -0.0436 -0.0043 -0.0456 145 ILE B O   
3449 C  CB  . ILE B 145 ? 0.0358 0.1389 0.1901 -0.0359 -0.0378 -0.0631 145 ILE B CB  
3450 C  CG1 . ILE B 145 ? 0.0337 0.1650 0.2129 -0.0165 -0.0466 -0.0680 145 ILE B CG1 
3451 C  CG2 . ILE B 145 ? 0.0447 0.1704 0.2735 -0.0314 -0.0702 -0.0805 145 ILE B CG2 
3452 C  CD1 . ILE B 145 ? 0.0430 0.1744 0.2356 -0.0497 -0.0571 -0.0409 145 ILE B CD1 
3453 N  N   . PHE B 146 ? 0.0170 0.1132 0.1169 -0.0275 -0.0071 -0.0427 146 PHE B N   
3454 C  CA  . PHE B 146 ? 0.0278 0.1136 0.1477 -0.0374 -0.0082 -0.0620 146 PHE B CA  
3455 C  C   . PHE B 146 ? 0.0289 0.1220 0.1631 -0.0456 0.0001  -0.0608 146 PHE B C   
3456 O  O   . PHE B 146 ? 0.0261 0.1522 0.1779 -0.0486 -0.0042 -0.0559 146 PHE B O   
3457 C  CB  . PHE B 146 ? 0.0224 0.1389 0.1447 -0.0420 -0.0052 -0.0413 146 PHE B CB  
3458 C  CG  . PHE B 146 ? 0.0245 0.0881 0.1230 -0.0343 -0.0035 -0.0381 146 PHE B CG  
3459 C  CD1 . PHE B 146 ? 0.0133 0.0996 0.1263 -0.0188 -0.0053 -0.0555 146 PHE B CD1 
3460 C  CD2 . PHE B 146 ? 0.0293 0.1117 0.1405 -0.0490 0.0110  -0.0309 146 PHE B CD2 
3461 C  CE1 . PHE B 146 ? 0.0428 0.0968 0.1270 -0.0456 -0.0079 -0.0528 146 PHE B CE1 
3462 C  CE2 . PHE B 146 ? 0.0369 0.1190 0.1606 -0.0585 0.0160  -0.0398 146 PHE B CE2 
3463 C  CZ  . PHE B 146 ? 0.0364 0.1002 0.1499 -0.0522 0.0176  -0.0507 146 PHE B CZ  
3464 N  N   . LEU B 147 ? 0.0476 0.1079 0.1474 -0.0565 -0.0055 -0.0507 147 LEU B N   
3465 C  CA  . LEU B 147 ? 0.0439 0.1127 0.1482 -0.0442 -0.0262 -0.0513 147 LEU B CA  
3466 C  C   . LEU B 147 ? 0.0217 0.1062 0.1535 -0.0389 0.0154  -0.0522 147 LEU B C   
3467 O  O   . LEU B 147 ? 0.0221 0.1064 0.1610 -0.0386 0.0076  -0.0476 147 LEU B O   
3468 C  CB  . LEU B 147 ? 0.0266 0.1207 0.1731 -0.0432 -0.0022 -0.0554 147 LEU B CB  
3469 C  CG  . LEU B 147 ? 0.1112 0.1161 0.1471 -0.0697 -0.0387 -0.0476 147 LEU B CG  
3470 C  CD1 . LEU B 147 ? 0.0967 0.1148 0.1432 -0.0802 -0.0301 -0.0375 147 LEU B CD1 
3471 C  CD2 . LEU B 147 ? 0.0793 0.1373 0.1614 -0.0578 -0.0387 -0.0402 147 LEU B CD2 
3472 N  N   . LYS B 148 ? 0.0265 0.1071 0.1533 -0.0398 -0.0068 -0.0439 148 LYS B N   
3473 C  CA  . LYS B 148 ? 0.0178 0.1226 0.1560 -0.0335 0.0048  -0.0372 148 LYS B CA  
3474 C  C   . LYS B 148 ? 0.0303 0.1025 0.1514 -0.0346 0.0013  -0.0447 148 LYS B C   
3475 O  O   . LYS B 148 ? 0.0674 0.1184 0.1738 -0.0201 -0.0165 -0.0487 148 LYS B O   
3476 C  CB  . LYS B 148 ? 0.0371 0.1739 0.1702 -0.0499 0.0130  -0.0297 148 LYS B CB  
3477 C  CG  . LYS B 148 ? 0.0393 0.2019 0.2226 -0.0567 0.0587  -0.0259 148 LYS B CG  
3478 C  CD  . LYS B 148 ? 0.1211 0.1952 0.2316 -0.0433 0.0635  -0.0071 148 LYS B CD  
3479 C  CE  . LYS B 148 ? 0.1749 0.4023 0.3640 -0.1155 0.0033  -0.0116 148 LYS B CE  
3480 N  NZ  . LYS B 148 ? 0.3367 0.5207 0.4589 -0.0161 0.1085  0.0392  148 LYS B NZ  
3481 N  N   . VAL B 149 ? 0.0590 0.0877 0.2037 -0.0444 -0.0266 -0.0631 149 VAL B N   
3482 C  CA  . VAL B 149 ? 0.0671 0.1102 0.1914 -0.0601 0.0190  -0.0672 149 VAL B CA  
3483 C  C   . VAL B 149 ? 0.0593 0.1192 0.1941 -0.0583 0.0001  -0.0531 149 VAL B C   
3484 O  O   . VAL B 149 ? 0.1139 0.1472 0.1814 -0.0697 -0.0221 -0.0409 149 VAL B O   
3485 C  CB  . VAL B 149 ? 0.0809 0.1426 0.1879 -0.0322 -0.0001 -0.0716 149 VAL B CB  
3486 C  CG1 . VAL B 149 ? 0.0617 0.2530 0.2312 -0.0996 -0.0186 -0.0883 149 VAL B CG1 
3487 C  CG2 . VAL B 149 ? 0.0559 0.1665 0.2287 -0.0572 0.0104  -0.0672 149 VAL B CG2 
3488 N  N   . GLY B 150 ? 0.0682 0.1073 0.1981 -0.0531 -0.0151 -0.0643 150 GLY B N   
3489 C  CA  . GLY B 150 ? 0.1046 0.1573 0.2201 -0.0950 -0.0193 -0.0445 150 GLY B CA  
3490 C  C   . GLY B 150 ? 0.0674 0.1794 0.2046 -0.0973 0.0125  -0.0488 150 GLY B C   
3491 O  O   . GLY B 150 ? 0.0439 0.1628 0.2218 -0.0741 0.0140  -0.0490 150 GLY B O   
3492 N  N   . SER B 151 ? 0.0629 0.1735 0.2183 -0.0906 -0.0089 -0.0414 151 SER B N   
3493 C  CA  . SER B 151 ? 0.0681 0.1734 0.2818 -0.0692 -0.0370 -0.0510 151 SER B CA  
3494 C  C   . SER B 151 ? 0.0873 0.1345 0.2194 -0.0675 -0.0363 -0.0741 151 SER B C   
3495 O  O   . SER B 151 ? 0.1033 0.1752 0.1929 -0.1152 -0.0183 -0.0526 151 SER B O   
3496 C  CB  . SER B 151 ? 0.0798 0.2732 0.4287 -0.0885 -0.0020 0.0091  151 SER B CB  
3497 O  OG  . SER B 151 ? 0.2703 0.3747 0.4344 -0.1090 0.0563  0.0566  151 SER B OG  
3498 N  N   . ALA B 152 ? 0.0904 0.1357 0.2189 -0.0573 -0.0443 -0.0639 152 ALA B N   
3499 C  CA  . ALA B 152 ? 0.1553 0.1039 0.2281 -0.0496 -0.0766 -0.0837 152 ALA B CA  
3500 C  C   . ALA B 152 ? 0.0908 0.1156 0.2386 -0.0410 -0.0729 -0.0753 152 ALA B C   
3501 O  O   . ALA B 152 ? 0.1028 0.1401 0.2788 -0.0204 -0.0619 -0.0954 152 ALA B O   
3502 C  CB  . ALA B 152 ? 0.2368 0.1497 0.2225 -0.0402 -0.0972 -0.0642 152 ALA B CB  
3503 N  N   . LYS B 153 ? 0.1421 0.0996 0.2069 -0.0443 -0.0803 -0.0634 153 LYS B N   
3504 C  CA  . LYS B 153 ? 0.1377 0.1132 0.2321 -0.0457 -0.0769 -0.0910 153 LYS B CA  
3505 C  C   . LYS B 153 ? 0.1195 0.1399 0.2671 0.0055  -0.0554 -0.0794 153 LYS B C   
3506 O  O   . LYS B 153 ? 0.1242 0.2039 0.2318 -0.0207 -0.1109 -0.0965 153 LYS B O   
3507 C  CB  . LYS B 153 ? 0.1213 0.1129 0.2687 -0.0603 -0.0785 -0.0669 153 LYS B CB  
3508 C  CG  . LYS B 153 ? 0.2522 0.1156 0.2761 -0.0427 -0.1221 -0.0945 153 LYS B CG  
3509 C  CD  . LYS B 153 ? 0.2828 0.1438 0.2816 -0.0276 -0.1064 -0.0946 153 LYS B CD  
3510 C  CE  . LYS B 153 ? 0.3198 0.1771 0.2314 -0.0501 -0.0600 -0.0882 153 LYS B CE  
3511 N  NZ  . LYS B 153 ? 0.0798 0.3084 0.3764 -0.0348 -0.0375 -0.0615 153 LYS B NZ  
3512 N  N   . PRO B 154 ? 0.1229 0.1498 0.2518 -0.0215 -0.0647 -0.0697 154 PRO B N   
3513 C  CA  . PRO B 154 ? 0.0917 0.1976 0.3067 -0.0517 -0.0973 -0.0099 154 PRO B CA  
3514 C  C   . PRO B 154 ? 0.1478 0.1599 0.2637 -0.0177 -0.0983 -0.0541 154 PRO B C   
3515 O  O   . PRO B 154 ? 0.2261 0.1764 0.2943 -0.0571 -0.1426 -0.0311 154 PRO B O   
3516 C  CB  . PRO B 154 ? 0.1000 0.2062 0.2979 -0.0542 -0.1040 -0.0212 154 PRO B CB  
3517 C  CG  . PRO B 154 ? 0.1870 0.3565 0.2630 0.0034  -0.0988 0.0337  154 PRO B CG  
3518 C  CD  . PRO B 154 ? 0.1251 0.1865 0.2667 -0.0486 -0.0670 -0.0450 154 PRO B CD  
3519 N  N   . GLY B 155 ? 0.1473 0.1685 0.2437 0.0057  -0.0914 -0.0542 155 GLY B N   
3520 C  CA  . GLY B 155 ? 0.1703 0.2005 0.3267 -0.0441 -0.0873 -0.0658 155 GLY B CA  
3521 C  C   . GLY B 155 ? 0.2178 0.1467 0.2630 -0.0365 -0.0471 -0.0159 155 GLY B C   
3522 O  O   . GLY B 155 ? 0.2812 0.1209 0.3248 -0.0475 -0.0483 -0.0334 155 GLY B O   
3523 N  N   . LEU B 156 ? 0.1687 0.1133 0.2730 -0.0475 -0.0656 -0.0827 156 LEU B N   
3524 C  CA  . LEU B 156 ? 0.1706 0.1091 0.2333 -0.0703 -0.0653 -0.0543 156 LEU B CA  
3525 C  C   . LEU B 156 ? 0.2735 0.1782 0.2425 -0.1043 -0.1111 -0.0591 156 LEU B C   
3526 O  O   . LEU B 156 ? 0.2895 0.1328 0.2014 -0.0458 -0.1285 -0.0701 156 LEU B O   
3527 C  CB  . LEU B 156 ? 0.1825 0.1309 0.2647 -0.0988 -0.1157 -0.0365 156 LEU B CB  
3528 C  CG  . LEU B 156 ? 0.1800 0.1576 0.2049 -0.0899 -0.0927 -0.0359 156 LEU B CG  
3529 C  CD1 . LEU B 156 ? 0.2238 0.1410 0.2229 -0.0767 -0.1030 -0.0666 156 LEU B CD1 
3530 C  CD2 . LEU B 156 ? 0.0809 0.1663 0.2201 -0.0628 -0.0411 -0.0324 156 LEU B CD2 
3531 N  N   . GLN B 157 ? 0.2403 0.1498 0.2269 -0.0663 -0.1177 -0.0471 157 GLN B N   
3532 C  CA  . GLN B 157 ? 0.2893 0.1538 0.2194 -0.0884 -0.1042 -0.0674 157 GLN B CA  
3533 C  C   . GLN B 157 ? 0.1775 0.2212 0.1747 -0.0425 -0.0983 -0.0657 157 GLN B C   
3534 O  O   . GLN B 157 ? 0.2593 0.1518 0.1983 -0.0432 -0.0870 -0.0837 157 GLN B O   
3535 C  CB  . GLN B 157 ? 0.2978 0.1706 0.2349 -0.1053 -0.0983 -0.0602 157 GLN B CB  
3536 C  CG  . GLN B 157 ? 0.3828 0.1638 0.2026 -0.0706 -0.1120 -0.0512 157 GLN B CG  
3537 C  CD  . GLN B 157 ? 0.3641 0.1507 0.2237 -0.0912 -0.1050 -0.0367 157 GLN B CD  
3538 O  OE1 . GLN B 157 ? 0.3863 0.1487 0.2248 -0.1339 -0.1127 -0.0340 157 GLN B OE1 
3539 N  NE2 . GLN B 157 ? 0.3952 0.2122 0.2374 -0.1135 -0.1454 -0.1088 157 GLN B NE2 
3540 N  N   . LYS B 158 ? 0.2645 0.1802 0.2361 -0.0525 -0.1273 -0.0414 158 LYS B N   
3541 C  CA  . LYS B 158 ? 0.2242 0.2058 0.2148 -0.0468 -0.1033 -0.0526 158 LYS B CA  
3542 C  C   . LYS B 158 ? 0.2059 0.1315 0.2119 -0.0795 -0.0836 -0.0530 158 LYS B C   
3543 O  O   . LYS B 158 ? 0.3097 0.1439 0.2284 -0.1181 -0.0878 -0.0249 158 LYS B O   
3544 C  CB  . LYS B 158 ? 0.2868 0.1845 0.2185 -0.0347 -0.0974 -0.0666 158 LYS B CB  
3545 C  CG  . LYS B 158 ? 0.2748 0.3676 0.4207 -0.0885 -0.1504 -0.0277 158 LYS B CG  
3546 N  N   . VAL B 159 ? 0.3133 0.0978 0.2335 -0.0554 -0.1389 -0.0785 159 VAL B N   
3547 C  CA  . VAL B 159 ? 0.3057 0.1448 0.1562 -0.0981 -0.0577 -0.0476 159 VAL B CA  
3548 C  C   . VAL B 159 ? 0.3344 0.1420 0.1460 -0.0558 -0.0993 -0.0317 159 VAL B C   
3549 O  O   . VAL B 159 ? 0.3149 0.1355 0.1693 -0.0490 -0.0949 -0.0436 159 VAL B O   
3550 C  CB  . VAL B 159 ? 0.2974 0.1701 0.1809 -0.0682 -0.1263 -0.0657 159 VAL B CB  
3551 C  CG1 . VAL B 159 ? 0.3067 0.1937 0.1975 -0.0817 -0.1423 -0.0337 159 VAL B CG1 
3552 C  CG2 . VAL B 159 ? 0.3305 0.1786 0.2452 -0.0257 -0.1372 -0.0805 159 VAL B CG2 
3553 N  N   . VAL B 160 ? 0.2442 0.1317 0.1983 -0.0571 -0.1024 -0.0601 160 VAL B N   
3554 C  CA  . VAL B 160 ? 0.2639 0.1660 0.2397 -0.0453 -0.0869 -0.0590 160 VAL B CA  
3555 C  C   . VAL B 160 ? 0.3012 0.1217 0.2247 -0.0624 -0.0613 -0.0695 160 VAL B C   
3556 O  O   . VAL B 160 ? 0.3152 0.1235 0.2407 -0.0635 -0.0775 -0.0776 160 VAL B O   
3557 C  CB  . VAL B 160 ? 0.5014 0.1656 0.2356 0.0139  0.0527  -0.0174 160 VAL B CB  
3558 C  CG1 . VAL B 160 ? 0.4660 0.2514 0.4017 -0.0125 -0.0359 -0.1017 160 VAL B CG1 
3559 C  CG2 . VAL B 160 ? 0.4693 0.2149 0.2755 0.0673  0.0250  -0.0082 160 VAL B CG2 
3560 N  N   . ASP B 161 ? 0.3145 0.1553 0.1985 -0.0744 -0.0879 -0.0544 161 ASP B N   
3561 C  CA  . ASP B 161 ? 0.3536 0.1569 0.1911 -0.0719 -0.0805 -0.0840 161 ASP B CA  
3562 C  C   . ASP B 161 ? 0.4119 0.1978 0.2149 -0.1018 -0.1206 -0.0547 161 ASP B C   
3563 O  O   . ASP B 161 ? 0.6053 0.2175 0.2086 -0.1390 -0.0994 -0.0703 161 ASP B O   
3564 C  CB  . ASP B 161 ? 0.3917 0.2805 0.2101 -0.1012 -0.1249 -0.0796 161 ASP B CB  
3565 C  CG  . ASP B 161 ? 0.3834 0.2251 0.2653 -0.0372 -0.0860 -0.1338 161 ASP B CG  
3566 O  OD1 . ASP B 161 ? 0.3133 0.2309 0.3491 -0.0829 -0.0897 -0.0672 161 ASP B OD1 
3567 O  OD2 . ASP B 161 ? 0.3617 0.3842 0.3667 0.0447  -0.1433 -0.1392 161 ASP B OD2 
3568 N  N   . VAL B 162 ? 0.4171 0.1490 0.1727 -0.1024 -0.1124 -0.0206 162 VAL B N   
3569 C  CA  . VAL B 162 ? 0.4316 0.2117 0.1901 -0.1066 -0.1077 -0.0023 162 VAL B CA  
3570 C  C   . VAL B 162 ? 0.4405 0.1263 0.2023 -0.0869 -0.0617 -0.0431 162 VAL B C   
3571 O  O   . VAL B 162 ? 0.5240 0.2085 0.1805 -0.1641 -0.0741 -0.0325 162 VAL B O   
3572 C  CB  . VAL B 162 ? 0.4903 0.2012 0.3162 -0.0497 -0.1747 -0.0020 162 VAL B CB  
3573 C  CG1 . VAL B 162 ? 0.5705 0.1288 0.3008 -0.0653 -0.1662 -0.0306 162 VAL B CG1 
3574 C  CG2 . VAL B 162 ? 0.5779 0.3245 0.3326 0.0245  -0.0671 0.0542  162 VAL B CG2 
3575 N  N   . LEU B 163 ? 0.4111 0.1526 0.1884 -0.1089 -0.0829 -0.0658 163 LEU B N   
3576 C  CA  . LEU B 163 ? 0.3736 0.1614 0.1672 -0.1098 -0.0374 -0.0499 163 LEU B CA  
3577 C  C   . LEU B 163 ? 0.3651 0.1237 0.1729 -0.1064 -0.0195 -0.0388 163 LEU B C   
3578 O  O   . LEU B 163 ? 0.4319 0.1923 0.2058 -0.2010 -0.0182 -0.0335 163 LEU B O   
3579 C  CB  . LEU B 163 ? 0.2924 0.1590 0.1679 -0.1119 -0.0187 -0.0496 163 LEU B CB  
3580 C  CG  . LEU B 163 ? 0.2538 0.1247 0.1758 -0.0864 -0.0252 -0.0601 163 LEU B CG  
3581 C  CD1 . LEU B 163 ? 0.2400 0.1542 0.1843 -0.0945 0.0151  -0.0190 163 LEU B CD1 
3582 C  CD2 . LEU B 163 ? 0.2547 0.1490 0.1891 -0.0987 -0.0566 -0.0678 163 LEU B CD2 
3583 N  N   . ASP B 164 ? 0.4689 0.1711 0.1442 -0.1061 -0.0141 -0.0557 164 ASP B N   
3584 C  CA  . ASP B 164 ? 0.5687 0.1486 0.1810 -0.1090 0.0325  -0.0847 164 ASP B CA  
3585 C  C   . ASP B 164 ? 0.5147 0.2450 0.2010 -0.1410 -0.0204 -0.0005 164 ASP B C   
3586 O  O   . ASP B 164 ? 0.5268 0.3095 0.2448 -0.1668 0.0211  -0.0198 164 ASP B O   
3587 C  CB  . ASP B 164 ? 0.5123 0.2297 0.2804 -0.1938 -0.0102 -0.0789 164 ASP B CB  
3588 C  CG  . ASP B 164 ? 0.5506 0.5238 0.5218 -0.0596 0.0610  0.0239  164 ASP B CG  
3589 O  OD1 . ASP B 164 ? 0.7565 0.3811 0.3116 -0.2461 0.0516  -0.0967 164 ASP B OD1 
3590 O  OD2 . ASP B 164 ? 0.7130 0.8907 0.5143 -0.2242 0.1025  -0.1459 164 ASP B OD2 
3591 N  N   . SER B 165 ? 0.4627 0.2264 0.1649 -0.1694 -0.0862 -0.0250 165 SER B N   
3592 C  CA  . SER B 165 ? 0.5721 0.2076 0.1533 -0.1522 -0.0323 -0.0223 165 SER B CA  
3593 C  C   . SER B 165 ? 0.5331 0.1910 0.2031 -0.1273 -0.0301 -0.0323 165 SER B C   
3594 O  O   . SER B 165 ? 0.6365 0.2191 0.1744 -0.2006 -0.0756 -0.0316 165 SER B O   
3595 C  CB  . SER B 165 ? 0.6301 0.1866 0.1858 -0.1372 -0.0414 -0.0143 165 SER B CB  
3596 O  OG  . SER B 165 ? 0.5841 0.2387 0.2177 -0.0780 -0.0985 -0.0370 165 SER B OG  
3597 N  N   . ILE B 166 ? 0.5369 0.1707 0.2134 -0.1360 -0.0055 0.0269  166 ILE B N   
3598 C  CA  . ILE B 166 ? 0.5345 0.1857 0.1829 -0.1379 0.0314  0.0063  166 ILE B CA  
3599 C  C   . ILE B 166 ? 0.4221 0.1702 0.1549 -0.1697 0.0143  -0.0502 166 ILE B C   
3600 O  O   . ILE B 166 ? 0.4862 0.1869 0.1504 -0.2006 0.0147  -0.0580 166 ILE B O   
3601 C  CB  . ILE B 166 ? 0.4553 0.1839 0.2010 -0.1824 -0.0085 -0.0323 166 ILE B CB  
3602 C  CG1 . ILE B 166 ? 0.3882 0.2154 0.1434 -0.1909 -0.0403 -0.0469 166 ILE B CG1 
3603 C  CG2 . ILE B 166 ? 0.4916 0.1983 0.1941 -0.1514 -0.0638 -0.0428 166 ILE B CG2 
3604 C  CD1 . ILE B 166 ? 0.3549 0.2155 0.1507 -0.0725 -0.0311 -0.0751 166 ILE B CD1 
3605 N  N   . LYS B 167 ? 0.4410 0.1868 0.1606 -0.1688 0.0268  -0.0516 167 LYS B N   
3606 C  CA  . LYS B 167 ? 0.4082 0.1795 0.1676 -0.1843 0.0055  -0.0752 167 LYS B CA  
3607 C  C   . LYS B 167 ? 0.4509 0.1524 0.1869 -0.1611 0.0029  -0.0593 167 LYS B C   
3608 O  O   . LYS B 167 ? 0.4199 0.1743 0.1555 -0.1901 -0.0030 -0.0488 167 LYS B O   
3609 C  CB  . LYS B 167 ? 0.3152 0.2535 0.1503 -0.1816 0.0375  -0.0845 167 LYS B CB  
3610 C  CG  . LYS B 167 ? 0.2179 0.2951 0.2289 -0.1715 0.0597  -0.1275 167 LYS B CG  
3611 C  CD  . LYS B 167 ? 0.4925 0.3227 0.3230 -0.0295 -0.0781 -0.2175 167 LYS B CD  
3612 C  CE  . LYS B 167 ? 0.4262 0.5499 0.3053 0.0333  -0.0066 -0.1556 167 LYS B CE  
3613 N  NZ  . LYS B 167 ? 0.4707 0.8487 0.4370 -0.0992 -0.1109 -0.3747 167 LYS B NZ  
3614 N  N   . THR B 168 ? 0.4612 0.2009 0.1743 -0.2039 0.0183  -0.0414 168 THR B N   
3615 C  CA  . THR B 168 ? 0.4405 0.1829 0.1523 -0.2006 0.0467  -0.0895 168 THR B CA  
3616 C  C   . THR B 168 ? 0.2075 0.1538 0.1062 -0.1076 0.0589  -0.0515 168 THR B C   
3617 O  O   . THR B 168 ? 0.3609 0.1971 0.1961 -0.1129 -0.0020 0.0023  168 THR B O   
3618 C  CB  . THR B 168 ? 0.3506 0.2023 0.2374 -0.1896 0.0167  -0.0589 168 THR B CB  
3619 O  OG1 . THR B 168 ? 0.4239 0.2334 0.1809 -0.1684 0.0472  -0.0293 168 THR B OG1 
3620 C  CG2 . THR B 168 ? 0.3836 0.2375 0.1918 -0.1383 0.0636  -0.0342 168 THR B CG2 
3621 N  N   . LYS B 169 ? 0.2866 0.2119 0.1660 -0.1687 0.0353  -0.0343 169 LYS B N   
3622 C  CA  . LYS B 169 ? 0.4892 0.1850 0.1485 -0.1354 0.0133  -0.0505 169 LYS B CA  
3623 C  C   . LYS B 169 ? 0.4137 0.2165 0.1791 -0.2113 0.0098  0.0124  169 LYS B C   
3624 O  O   . LYS B 169 ? 0.5493 0.3210 0.1689 -0.2421 0.0351  -0.0479 169 LYS B O   
3625 C  CB  . LYS B 169 ? 0.4637 0.2009 0.1550 -0.1173 0.0812  -0.0531 169 LYS B CB  
3626 C  CG  . LYS B 169 ? 0.3838 0.2222 0.1960 -0.1804 0.1106  -0.0439 169 LYS B CG  
3627 C  CD  . LYS B 169 ? 0.5617 0.4973 0.4755 -0.0939 0.0033  -0.0439 169 LYS B CD  
3628 C  CE  . LYS B 169 ? 0.7349 1.0295 0.4433 0.2134  -0.0474 -0.3000 169 LYS B CE  
3629 N  NZ  . LYS B 169 ? 0.5316 0.7142 0.8663 -0.0797 0.3669  0.4062  169 LYS B NZ  
3630 N  N   . GLY B 170 ? 0.5471 0.2069 0.2044 -0.2113 0.0113  -0.0184 170 GLY B N   
3631 C  CA  . GLY B 170 ? 0.5598 0.2345 0.2511 -0.2336 -0.0706 0.0342  170 GLY B CA  
3632 C  C   . GLY B 170 ? 0.5041 0.2180 0.2024 -0.2282 -0.0458 -0.0403 170 GLY B C   
3633 O  O   . GLY B 170 ? 0.6418 0.2699 0.1996 -0.2161 -0.0395 0.0036  170 GLY B O   
3634 N  N   . LYS B 171 ? 0.2075 0.2464 0.3096 -0.1420 0.0206  0.0221  171 LYS B N   
3635 C  CA  . LYS B 171 ? 0.3780 0.2678 0.2758 -0.2850 -0.0529 -0.0651 171 LYS B CA  
3636 C  C   . LYS B 171 ? 0.2630 0.1970 0.3142 -0.0578 -0.1104 -0.0683 171 LYS B C   
3637 O  O   . LYS B 171 ? 0.4062 0.1978 0.2473 -0.1414 -0.0725 0.0033  171 LYS B O   
3638 C  CB  . LYS B 171 ? 0.3677 0.1646 0.3369 -0.1518 -0.0296 -0.1161 171 LYS B CB  
3639 C  CG  . LYS B 171 ? 0.3811 0.2915 0.4914 -0.1608 0.0197  -0.0569 171 LYS B CG  
3640 C  CD  . LYS B 171 ? 0.6302 0.3616 0.4420 -0.2022 0.0282  -0.0261 171 LYS B CD  
3641 C  CE  . LYS B 171 ? 0.7169 0.6551 0.5735 0.0238  0.1470  0.0329  171 LYS B CE  
3642 N  NZ  . LYS B 171 ? 0.5606 0.5189 0.5774 -0.1949 0.0595  0.0280  171 LYS B NZ  
3643 N  N   A SER B 172 ? 0.0943 0.2645 0.2999 -0.0168 0.1533  0.0521  172 SER B N   
3644 N  N   B SER B 172 ? 0.1221 0.2081 0.2560 -0.0855 -0.1011 -0.0748 172 SER B N   
3645 C  CA  A SER B 172 ? 0.0445 0.3716 0.3361 -0.0683 0.0984  -0.0410 172 SER B CA  
3646 C  CA  B SER B 172 ? 0.0829 0.3429 0.3680 -0.1361 -0.0344 0.0171  172 SER B CA  
3647 C  C   A SER B 172 ? 0.0403 0.2459 0.3966 -0.0785 -0.0096 0.0728  172 SER B C   
3648 C  C   B SER B 172 ? 0.0485 0.2512 0.3087 -0.0891 -0.0156 0.0757  172 SER B C   
3649 O  O   A SER B 172 ? 0.0405 0.4462 0.3454 -0.0038 0.0832  0.0524  172 SER B O   
3650 O  O   B SER B 172 ? 0.4823 0.3098 0.2487 -0.0055 0.0059  0.0177  172 SER B O   
3651 C  CB  A SER B 172 ? 0.0186 0.3245 0.3403 0.0198  -0.0065 -0.1305 172 SER B CB  
3652 C  CB  B SER B 172 ? 0.0594 0.3276 0.3753 -0.1045 0.0862  -0.0073 172 SER B CB  
3653 O  OG  A SER B 172 ? 0.0536 0.2224 0.2523 -0.0150 0.0394  -0.1077 172 SER B OG  
3654 O  OG  B SER B 172 ? 0.0484 0.2396 0.4226 -0.0719 -0.0305 -0.0008 172 SER B OG  
3655 N  N   . ALA B 173 ? 0.0568 0.2754 0.4828 -0.0741 0.0496  -0.1226 173 ALA B N   
3656 C  CA  . ALA B 173 ? 0.0475 0.4272 0.3407 0.0030  0.0823  0.1027  173 ALA B CA  
3657 C  C   . ALA B 173 ? 0.0414 0.2981 0.2908 -0.0939 -0.0212 0.0227  173 ALA B C   
3658 O  O   . ALA B 173 ? 0.0674 0.3380 0.2327 -0.0067 -0.0179 -0.0240 173 ALA B O   
3659 C  CB  . ALA B 173 ? 0.5021 0.3414 0.2329 0.1085  -0.0804 -0.1004 173 ALA B CB  
3660 N  N   . ASP B 174 ? 0.0816 0.5121 0.2766 0.1005  0.0039  0.0175  174 ASP B N   
3661 C  CA  . ASP B 174 ? 0.0653 0.4560 0.2486 -0.0814 0.0846  -0.0994 174 ASP B CA  
3662 C  C   . ASP B 174 ? 0.1972 0.3655 0.3782 0.0950  0.1410  0.0585  174 ASP B C   
3663 O  O   . ASP B 174 ? 0.4962 0.3650 0.3324 0.1865  -0.1259 -0.0988 174 ASP B O   
3664 C  CB  . ASP B 174 ? 0.1699 0.7350 0.4740 0.0725  -0.0187 0.0730  174 ASP B CB  
3665 C  CG  . ASP B 174 ? 0.2576 0.7754 0.5774 -0.1476 -0.0312 0.0106  174 ASP B CG  
3666 O  OD1 . ASP B 174 ? 0.3256 0.7851 0.5316 -0.0214 -0.1848 -0.0674 174 ASP B OD1 
3667 O  OD2 . ASP B 174 ? 0.4125 0.9796 0.5483 -0.2456 0.0059  -0.1067 174 ASP B OD2 
3668 N  N   . PHE B 175 ? 0.0822 0.3898 0.2643 -0.1046 -0.0080 -0.0930 175 PHE B N   
3669 C  CA  . PHE B 175 ? 0.3656 0.2490 0.1646 -0.0675 -0.0832 -0.0559 175 PHE B CA  
3670 C  C   . PHE B 175 ? 0.3937 0.1742 0.3374 -0.0300 -0.1368 -0.0211 175 PHE B C   
3671 O  O   . PHE B 175 ? 0.6244 0.2288 0.3231 0.0513  -0.1368 -0.0268 175 PHE B O   
3672 C  CB  . PHE B 175 ? 0.5171 0.1681 0.2053 -0.0052 -0.1247 -0.0644 175 PHE B CB  
3673 C  CG  . PHE B 175 ? 0.4594 0.1709 0.2180 0.0011  -0.1498 -0.0472 175 PHE B CG  
3674 C  CD1 . PHE B 175 ? 0.4233 0.1855 0.2335 -0.0184 -0.1662 -0.0516 175 PHE B CD1 
3675 C  CD2 . PHE B 175 ? 0.3623 0.1782 0.2297 -0.0174 -0.1203 -0.0820 175 PHE B CD2 
3676 C  CE1 . PHE B 175 ? 0.5759 0.1261 0.2682 0.0302  -0.1525 -0.0377 175 PHE B CE1 
3677 C  CE2 . PHE B 175 ? 0.4636 0.1338 0.3146 -0.0061 -0.1948 -0.0564 175 PHE B CE2 
3678 C  CZ  . PHE B 175 ? 0.4204 0.1428 0.2856 -0.0462 -0.1109 -0.0636 175 PHE B CZ  
3679 N  N   A THR B 176 ? 0.3596 0.1596 0.2804 -0.1294 -0.1359 0.0104  176 THR B N   
3680 N  N   B THR B 176 ? 0.4328 0.2430 0.2357 -0.0752 -0.1391 -0.0022 176 THR B N   
3681 C  CA  A THR B 176 ? 0.4156 0.1096 0.2893 -0.1082 -0.1530 0.0036  176 THR B CA  
3682 C  CA  B THR B 176 ? 0.4759 0.2088 0.2588 -0.0482 -0.1503 0.0168  176 THR B CA  
3683 C  C   A THR B 176 ? 0.3605 0.1487 0.2272 -0.1289 -0.2025 -0.0264 176 THR B C   
3684 C  C   B THR B 176 ? 0.4456 0.1429 0.2079 -0.0719 -0.2107 -0.0146 176 THR B C   
3685 O  O   A THR B 176 ? 0.3750 0.1164 0.2669 -0.0855 -0.1434 -0.0289 176 THR B O   
3686 O  O   B THR B 176 ? 0.3888 0.1450 0.2527 -0.0937 -0.1350 -0.0265 176 THR B O   
3687 C  CB  A THR B 176 ? 0.3898 0.1395 0.3386 -0.0759 -0.2020 0.0135  176 THR B CB  
3688 C  CB  B THR B 176 ? 0.5213 0.2239 0.2540 -0.0362 -0.2073 0.0006  176 THR B CB  
3689 O  OG1 A THR B 176 ? 0.2967 0.2046 0.3175 -0.1111 -0.1691 0.0258  176 THR B OG1 
3690 O  OG1 B THR B 176 ? 0.7665 0.3428 0.3455 0.0200  -0.0633 -0.0409 176 THR B OG1 
3691 C  CG2 A THR B 176 ? 0.5243 0.1091 0.3880 -0.1189 -0.2154 0.0119  176 THR B CG2 
3692 C  CG2 B THR B 176 ? 0.5942 0.2358 0.1388 0.0344  -0.1362 -0.0456 176 THR B CG2 
3693 N  N   . ASN B 177 ? 0.4266 0.1996 0.2395 -0.0813 -0.1867 0.0043  177 ASN B N   
3694 C  CA  . ASN B 177 ? 0.4026 0.1933 0.2197 -0.0580 -0.1834 -0.0245 177 ASN B CA  
3695 C  C   . ASN B 177 ? 0.4018 0.2019 0.2270 -0.0822 -0.1527 -0.0064 177 ASN B C   
3696 O  O   . ASN B 177 ? 0.3517 0.2152 0.3257 -0.0596 -0.1808 0.0221  177 ASN B O   
3697 C  CB  . ASN B 177 ? 0.3563 0.1852 0.2322 -0.0960 -0.1740 0.0260  177 ASN B CB  
3698 C  CG  . ASN B 177 ? 0.3944 0.1497 0.2224 -0.0320 -0.1518 -0.0467 177 ASN B CG  
3699 O  OD1 . ASN B 177 ? 0.3509 0.2496 0.2810 -0.0012 -0.1268 -0.0622 177 ASN B OD1 
3700 N  ND2 . ASN B 177 ? 0.3877 0.2057 0.2188 -0.0290 -0.1512 0.0041  177 ASN B ND2 
3701 N  N   . PHE B 178 ? 0.4386 0.1730 0.1830 -0.0666 -0.1650 -0.0097 178 PHE B N   
3702 C  CA  . PHE B 178 ? 0.4355 0.1629 0.2099 -0.0577 -0.1761 -0.0162 178 PHE B CA  
3703 C  C   . PHE B 178 ? 0.3395 0.1515 0.2110 -0.0650 -0.1742 -0.0110 178 PHE B C   
3704 O  O   . PHE B 178 ? 0.3257 0.1669 0.2564 -0.0800 -0.1705 -0.0354 178 PHE B O   
3705 C  CB  . PHE B 178 ? 0.4365 0.1147 0.1888 -0.0607 -0.0825 -0.0223 178 PHE B CB  
3706 C  CG  . PHE B 178 ? 0.3768 0.1608 0.1975 -0.0859 -0.1161 0.0048  178 PHE B CG  
3707 C  CD1 . PHE B 178 ? 0.3577 0.1632 0.2314 -0.0635 -0.1130 -0.0228 178 PHE B CD1 
3708 C  CD2 . PHE B 178 ? 0.2723 0.1547 0.2094 -0.0793 -0.1256 -0.0326 178 PHE B CD2 
3709 C  CE1 . PHE B 178 ? 0.4272 0.1807 0.2076 -0.0513 -0.0989 -0.0223 178 PHE B CE1 
3710 C  CE2 . PHE B 178 ? 0.2096 0.1595 0.1797 -0.0696 -0.0976 -0.0279 178 PHE B CE2 
3711 C  CZ  . PHE B 178 ? 0.2532 0.1398 0.2397 -0.0293 -0.1083 -0.0513 178 PHE B CZ  
3712 N  N   . ASP B 179 ? 0.2636 0.1639 0.2290 -0.0522 -0.1492 -0.0215 179 ASP B N   
3713 C  CA  . ASP B 179 ? 0.1429 0.2013 0.2638 -0.0723 -0.1151 -0.0161 179 ASP B CA  
3714 C  C   . ASP B 179 ? 0.1759 0.1240 0.2427 -0.0644 -0.1055 -0.0489 179 ASP B C   
3715 O  O   . ASP B 179 ? 0.2089 0.1247 0.2606 -0.0406 -0.1251 -0.0841 179 ASP B O   
3716 C  CB  . ASP B 179 ? 0.1261 0.2109 0.3683 -0.0368 -0.1108 -0.0102 179 ASP B CB  
3717 C  CG  . ASP B 179 ? 0.1649 0.3082 0.3418 -0.0110 -0.1468 0.0176  179 ASP B CG  
3718 O  OD1 . ASP B 179 ? 0.1694 0.1746 0.3446 -0.0278 -0.1279 -0.0086 179 ASP B OD1 
3719 O  OD2 . ASP B 179 ? 0.1412 0.5097 0.4158 -0.0145 -0.1258 -0.0032 179 ASP B OD2 
3720 N  N   . PRO B 180 ? 0.1046 0.1656 0.2288 -0.0646 -0.0833 -0.0376 180 PRO B N   
3721 C  CA  . PRO B 180 ? 0.1273 0.1559 0.2171 -0.0272 -0.0922 -0.0482 180 PRO B CA  
3722 C  C   . PRO B 180 ? 0.1373 0.1612 0.2002 -0.0146 -0.0978 -0.0462 180 PRO B C   
3723 O  O   . PRO B 180 ? 0.1055 0.1435 0.2107 -0.0100 -0.0627 -0.0486 180 PRO B O   
3724 C  CB  . PRO B 180 ? 0.1759 0.1518 0.2482 -0.0501 -0.0982 -0.0439 180 PRO B CB  
3725 C  CG  . PRO B 180 ? 0.1617 0.1587 0.2652 -0.0563 -0.1151 -0.0425 180 PRO B CG  
3726 C  CD  . PRO B 180 ? 0.2154 0.1565 0.2599 -0.0296 -0.1314 -0.0586 180 PRO B CD  
3727 N  N   . ARG B 181 ? 0.1138 0.1348 0.2268 -0.0436 -0.0877 -0.0434 181 ARG B N   
3728 C  CA  . ARG B 181 ? 0.0773 0.1398 0.2483 -0.0447 -0.0877 -0.0365 181 ARG B CA  
3729 C  C   . ARG B 181 ? 0.1391 0.1553 0.2489 -0.0284 -0.1443 -0.0357 181 ARG B C   
3730 O  O   . ARG B 181 ? 0.1452 0.2066 0.3061 -0.0107 -0.1220 -0.0001 181 ARG B O   
3731 C  CB  . ARG B 181 ? 0.0766 0.1986 0.2900 -0.0350 -0.0932 -0.0502 181 ARG B CB  
3732 C  CG  . ARG B 181 ? 0.1123 0.1856 0.3626 -0.0145 -0.0904 -0.0283 181 ARG B CG  
3733 C  CD  . ARG B 181 ? 0.1080 0.2359 0.4457 0.0049  0.0392  0.0385  181 ARG B CD  
3734 N  NE  . ARG B 181 ? 0.1690 0.2151 0.4667 0.0094  -0.0158 0.0657  181 ARG B NE  
3735 C  CZ  . ARG B 181 ? 0.1060 0.3653 0.4253 0.0208  0.0497  0.1303  181 ARG B CZ  
3736 N  NH1 . ARG B 181 ? 0.1536 0.4135 0.4938 -0.0334 0.1021  0.0790  181 ARG B NH1 
3737 N  NH2 . ARG B 181 ? 0.1676 0.3438 0.4863 -0.0255 -0.0766 0.0750  181 ARG B NH2 
3738 N  N   . GLY B 182 ? 0.1252 0.1568 0.2560 -0.0572 -0.1160 -0.0557 182 GLY B N   
3739 C  CA  . GLY B 182 ? 0.1739 0.1541 0.2990 -0.0197 -0.1605 -0.0637 182 GLY B CA  
3740 C  C   . GLY B 182 ? 0.1650 0.1715 0.2815 0.0006  -0.1398 -0.0726 182 GLY B C   
3741 O  O   . GLY B 182 ? 0.2404 0.1647 0.2797 0.0002  -0.1237 -0.0697 182 GLY B O   
3742 N  N   . LEU B 183 ? 0.1581 0.1636 0.2165 -0.0286 -0.0917 -0.0625 183 LEU B N   
3743 C  CA  . LEU B 183 ? 0.1494 0.1424 0.2079 -0.0355 -0.0685 -0.0627 183 LEU B CA  
3744 C  C   . LEU B 183 ? 0.1251 0.1398 0.2223 -0.0670 -0.0997 -0.0559 183 LEU B C   
3745 O  O   . LEU B 183 ? 0.1183 0.1587 0.2371 -0.0249 -0.0505 -0.0319 183 LEU B O   
3746 C  CB  . LEU B 183 ? 0.1249 0.1595 0.2123 -0.0105 -0.0340 -0.0255 183 LEU B CB  
3747 C  CG  . LEU B 183 ? 0.2852 0.1552 0.1991 -0.0336 -0.0513 -0.0390 183 LEU B CG  
3748 C  CD1 . LEU B 183 ? 0.2532 0.2587 0.2078 -0.0148 -0.0549 -0.0122 183 LEU B CD1 
3749 C  CD2 . LEU B 183 ? 0.2676 0.1945 0.2592 0.0119  -0.0412 -0.0739 183 LEU B CD2 
3750 N  N   A LEU B 184 ? 0.1173 0.1520 0.2626 -0.0253 -0.1018 -0.0539 184 LEU B N   
3751 N  N   B LEU B 184 ? 0.1661 0.1552 0.2621 -0.0060 -0.0883 -0.0551 184 LEU B N   
3752 C  CA  A LEU B 184 ? 0.0783 0.1653 0.2770 -0.0603 -0.1079 -0.0177 184 LEU B CA  
3753 C  CA  B LEU B 184 ? 0.1060 0.2109 0.2906 -0.0526 -0.1412 -0.0471 184 LEU B CA  
3754 C  C   A LEU B 184 ? 0.0748 0.1235 0.2828 -0.0556 -0.0840 0.0005  184 LEU B C   
3755 C  C   B LEU B 184 ? 0.0848 0.1851 0.2994 -0.0524 -0.1280 -0.0244 184 LEU B C   
3756 O  O   A LEU B 184 ? 0.1018 0.1651 0.3459 -0.0644 -0.1207 -0.0245 184 LEU B O   
3757 O  O   B LEU B 184 ? 0.2742 0.1599 0.3225 -0.1348 -0.2122 -0.0057 184 LEU B O   
3758 C  CB  A LEU B 184 ? 0.0448 0.1783 0.3474 -0.0496 -0.0879 -0.0091 184 LEU B CB  
3759 C  CB  B LEU B 184 ? 0.0564 0.2061 0.3169 -0.0566 -0.0920 -0.0350 184 LEU B CB  
3760 C  CG  A LEU B 184 ? 0.0429 0.1454 0.2392 -0.0451 -0.0690 -0.0073 184 LEU B CG  
3761 C  CG  B LEU B 184 ? 0.0617 0.1514 0.2520 -0.0656 -0.0387 -0.0458 184 LEU B CG  
3762 C  CD1 A LEU B 184 ? 0.0326 0.1810 0.2366 -0.0629 -0.0263 -0.0066 184 LEU B CD1 
3763 C  CD1 B LEU B 184 ? 0.0249 0.2220 0.2754 -0.0624 -0.0005 -0.0367 184 LEU B CD1 
3764 C  CD2 A LEU B 184 ? 0.0231 0.1175 0.2474 -0.0117 -0.0589 -0.0186 184 LEU B CD2 
3765 C  CD2 B LEU B 184 ? 0.0307 0.2267 0.1830 -0.0078 0.0085  -0.0398 184 LEU B CD2 
3766 N  N   . PRO B 185 ? 0.0647 0.1610 0.2500 -0.0532 -0.0807 -0.0252 185 PRO B N   
3767 C  CA  . PRO B 185 ? 0.0942 0.1355 0.2749 -0.0283 -0.0614 -0.0312 185 PRO B CA  
3768 C  C   . PRO B 185 ? 0.0605 0.3336 0.3694 -0.0763 -0.0487 0.0111  185 PRO B C   
3769 O  O   . PRO B 185 ? 0.2046 0.2260 0.6051 0.0469  0.0165  0.0541  185 PRO B O   
3770 C  CB  . PRO B 185 ? 0.0128 0.1467 0.2465 -0.0192 -0.0196 -0.0190 185 PRO B CB  
3771 C  CG  . PRO B 185 ? 0.0651 0.1464 0.2007 0.0065  -0.0211 -0.0476 185 PRO B CG  
3772 C  CD  . PRO B 185 ? 0.0418 0.1585 0.1816 -0.0512 -0.0312 -0.0455 185 PRO B CD  
3773 N  N   . GLU B 186 ? 0.0703 0.1355 0.4270 -0.0453 -0.0610 -0.0741 186 GLU B N   
3774 C  CA  . GLU B 186 ? 0.1183 0.2008 0.4823 0.0145  -0.0263 -0.0536 186 GLU B CA  
3775 C  C   . GLU B 186 ? 0.0221 0.1647 0.4178 -0.0473 -0.0195 -0.0207 186 GLU B C   
3776 O  O   . GLU B 186 ? 0.0669 0.2044 0.4623 -0.0211 -0.0201 -0.0444 186 GLU B O   
3777 C  CB  . GLU B 186 ? 0.2551 0.2735 0.5856 0.0115  -0.0319 0.1007  186 GLU B CB  
3778 C  CG  . GLU B 186 ? 0.4635 0.3609 0.5146 0.0617  -0.1166 -0.0097 186 GLU B CG  
3779 C  CD  . GLU B 186 ? 0.3291 0.3722 0.3771 0.0870  0.0238  -0.1022 186 GLU B CD  
3780 O  OE1 . GLU B 186 ? 0.3434 0.2597 0.6771 -0.0215 -0.0521 -0.0872 186 GLU B OE1 
3781 O  OE2 . GLU B 186 ? 0.3134 0.3526 0.4559 0.0606  0.0430  0.0513  186 GLU B OE2 
3782 N  N   . SER B 187 ? 0.0271 0.1813 0.4374 -0.0507 -0.0388 -0.0406 187 SER B N   
3783 C  CA  . SER B 187 ? 0.0242 0.2311 0.3990 -0.0573 0.0432  -0.0301 187 SER B CA  
3784 C  C   . SER B 187 ? 0.0180 0.1944 0.3833 -0.0463 0.0238  -0.0571 187 SER B C   
3785 O  O   . SER B 187 ? 0.0274 0.2079 0.3102 -0.0651 0.0398  -0.1057 187 SER B O   
3786 C  CB  . SER B 187 ? 0.1311 0.2448 0.4030 -0.1118 0.0348  -0.0322 187 SER B CB  
3787 O  OG  . SER B 187 ? 0.0507 0.2415 0.4388 -0.0596 0.0292  -0.0627 187 SER B OG  
3788 N  N   . LEU B 188 ? 0.0168 0.1951 0.3843 -0.0432 0.0000  -0.0675 188 LEU B N   
3789 C  CA  . LEU B 188 ? 0.0319 0.2081 0.3218 -0.0642 -0.0150 -0.0735 188 LEU B CA  
3790 C  C   . LEU B 188 ? 0.0335 0.2068 0.2666 -0.0716 0.0386  -0.0517 188 LEU B C   
3791 O  O   . LEU B 188 ? 0.0353 0.2160 0.3182 -0.0688 0.0321  -0.0888 188 LEU B O   
3792 C  CB  . LEU B 188 ? 0.0676 0.2010 0.4206 -0.1092 0.0231  -0.0399 188 LEU B CB  
3793 C  CG  . LEU B 188 ? 0.0317 0.2348 0.4528 0.0109  0.0343  -0.0237 188 LEU B CG  
3794 C  CD1 . LEU B 188 ? 0.1034 0.1996 0.5804 -0.0242 -0.0025 -0.1160 188 LEU B CD1 
3795 C  CD2 . LEU B 188 ? 0.0217 0.3230 0.4583 -0.0643 0.0243  0.0372  188 LEU B CD2 
3796 N  N   . ASP B 189 ? 0.0176 0.2081 0.2393 -0.0459 0.0303  -0.0761 189 ASP B N   
3797 C  CA  . ASP B 189 ? 0.0441 0.2386 0.2339 -0.0863 0.0436  -0.0212 189 ASP B CA  
3798 C  C   . ASP B 189 ? 0.0242 0.1603 0.2115 -0.0522 0.0182  -0.0675 189 ASP B C   
3799 O  O   . ASP B 189 ? 0.0304 0.1969 0.1973 -0.0677 0.0258  -0.0743 189 ASP B O   
3800 C  CB  . ASP B 189 ? 0.0911 0.2604 0.2360 -0.1192 -0.0027 -0.0245 189 ASP B CB  
3801 C  CG  . ASP B 189 ? 0.1191 0.4289 0.2309 -0.1342 0.0131  -0.0582 189 ASP B CG  
3802 O  OD1 . ASP B 189 ? 0.1269 0.5164 0.3797 -0.1570 0.1188  -0.1333 189 ASP B OD1 
3803 O  OD2 . ASP B 189 ? 0.2896 0.4689 0.4526 -0.1051 0.0388  0.0543  189 ASP B OD2 
3804 N  N   . TYR B 190 ? 0.0149 0.1574 0.1776 -0.0304 0.0299  -0.0529 190 TYR B N   
3805 C  CA  . TYR B 190 ? 0.0268 0.1372 0.1477 -0.0489 0.0332  -0.0449 190 TYR B CA  
3806 C  C   . TYR B 190 ? 0.0262 0.1568 0.1400 -0.0359 0.0417  -0.0269 190 TYR B C   
3807 O  O   . TYR B 190 ? 0.0310 0.1665 0.1535 -0.0547 0.0457  -0.0526 190 TYR B O   
3808 C  CB  . TYR B 190 ? 0.0512 0.1572 0.1660 -0.0124 0.0212  -0.0391 190 TYR B CB  
3809 C  CG  . TYR B 190 ? 0.0101 0.1663 0.1788 -0.0232 0.0146  -0.0457 190 TYR B CG  
3810 C  CD1 . TYR B 190 ? 0.0254 0.2457 0.2108 -0.0610 0.0420  -0.0649 190 TYR B CD1 
3811 C  CD2 . TYR B 190 ? 0.0170 0.1823 0.2120 -0.0383 0.0339  -0.0582 190 TYR B CD2 
3812 C  CE1 . TYR B 190 ? 0.0371 0.2243 0.2286 -0.0818 0.0188  -0.0439 190 TYR B CE1 
3813 C  CE2 . TYR B 190 ? 0.0394 0.1588 0.2149 -0.0421 0.0172  -0.0340 190 TYR B CE2 
3814 C  CZ  . TYR B 190 ? 0.0330 0.1731 0.2177 -0.0626 0.0412  -0.0435 190 TYR B CZ  
3815 O  OH  . TYR B 190 ? 0.0773 0.2015 0.2258 -0.0403 0.0281  -0.0710 190 TYR B OH  
3816 N  N   . TRP B 191 ? 0.0322 0.1278 0.1595 -0.0559 0.0167  -0.0432 191 TRP B N   
3817 C  CA  . TRP B 191 ? 0.0282 0.1247 0.1530 -0.0504 0.0302  -0.0531 191 TRP B CA  
3818 C  C   . TRP B 191 ? 0.0218 0.1103 0.1204 -0.0401 0.0137  -0.0362 191 TRP B C   
3819 O  O   . TRP B 191 ? 0.0309 0.1272 0.1330 -0.0544 0.0247  -0.0543 191 TRP B O   
3820 C  CB  . TRP B 191 ? 0.0500 0.1140 0.1602 -0.0394 0.0325  -0.0500 191 TRP B CB  
3821 C  CG  . TRP B 191 ? 0.0389 0.1388 0.1749 -0.0307 0.0435  -0.0233 191 TRP B CG  
3822 C  CD1 . TRP B 191 ? 0.0527 0.1323 0.1860 -0.0471 0.0304  -0.0296 191 TRP B CD1 
3823 C  CD2 . TRP B 191 ? 0.0241 0.1446 0.1691 -0.0370 0.0430  -0.0303 191 TRP B CD2 
3824 N  NE1 . TRP B 191 ? 0.1284 0.1407 0.1678 -0.0754 0.0249  -0.0331 191 TRP B NE1 
3825 C  CE2 . TRP B 191 ? 0.0200 0.1351 0.1768 -0.0346 0.0141  -0.0306 191 TRP B CE2 
3826 C  CE3 . TRP B 191 ? 0.0142 0.1634 0.1668 -0.0348 0.0153  -0.0478 191 TRP B CE3 
3827 C  CZ2 . TRP B 191 ? 0.0389 0.1486 0.2190 -0.0351 -0.0126 -0.0322 191 TRP B CZ2 
3828 C  CZ3 . TRP B 191 ? 0.0166 0.1679 0.2024 -0.0261 0.0422  -0.0611 191 TRP B CZ3 
3829 C  CH2 . TRP B 191 ? 0.0368 0.1559 0.2066 0.0005  0.0015  -0.0462 191 TRP B CH2 
3830 N  N   . THR B 192 ? 0.0257 0.1277 0.1335 -0.0486 0.0204  -0.0528 192 THR B N   
3831 C  CA  . THR B 192 ? 0.0186 0.1215 0.1268 -0.0368 0.0237  -0.0507 192 THR B CA  
3832 C  C   . THR B 192 ? 0.0183 0.1526 0.1247 -0.0351 0.0298  -0.0439 192 THR B C   
3833 O  O   . THR B 192 ? 0.0229 0.1474 0.1281 -0.0477 0.0227  -0.0481 192 THR B O   
3834 C  CB  . THR B 192 ? 0.0252 0.1158 0.1324 -0.0454 0.0254  -0.0636 192 THR B CB  
3835 O  OG1 . THR B 192 ? 0.0140 0.1184 0.1568 -0.0293 0.0137  -0.0588 192 THR B OG1 
3836 C  CG2 . THR B 192 ? 0.0529 0.1358 0.1393 -0.0114 0.0403  -0.0551 192 THR B CG2 
3837 N  N   . TYR B 193 ? 0.0206 0.1242 0.1406 -0.0407 0.0181  -0.0650 193 TYR B N   
3838 C  CA  . TYR B 193 ? 0.0207 0.1237 0.1282 -0.0400 0.0084  -0.0491 193 TYR B CA  
3839 C  C   . TYR B 193 ? 0.0189 0.0976 0.1168 -0.0337 0.0181  -0.0553 193 TYR B C   
3840 O  O   . TYR B 193 ? 0.0196 0.1175 0.1088 -0.0379 0.0143  -0.0584 193 TYR B O   
3841 C  CB  . TYR B 193 ? 0.0299 0.1147 0.1280 -0.0502 0.0123  -0.0374 193 TYR B CB  
3842 C  CG  . TYR B 193 ? 0.0216 0.0978 0.1249 -0.0348 0.0022  -0.0424 193 TYR B CG  
3843 C  CD1 . TYR B 193 ? 0.0113 0.1240 0.1299 -0.0201 -0.0035 -0.0514 193 TYR B CD1 
3844 C  CD2 . TYR B 193 ? 0.0216 0.1012 0.1266 -0.0356 0.0058  -0.0504 193 TYR B CD2 
3845 C  CE1 . TYR B 193 ? 0.0163 0.1146 0.1119 -0.0291 -0.0051 -0.0337 193 TYR B CE1 
3846 C  CE2 . TYR B 193 ? 0.0220 0.1262 0.1132 -0.0362 -0.0041 -0.0523 193 TYR B CE2 
3847 C  CZ  . TYR B 193 ? 0.0174 0.1217 0.1114 -0.0291 -0.0066 -0.0458 193 TYR B CZ  
3848 O  OH  . TYR B 193 ? 0.0157 0.1137 0.1191 -0.0314 0.0112  -0.0519 193 TYR B OH  
3849 N  N   . PRO B 194 ? 0.0152 0.1177 0.1134 -0.0295 0.0074  -0.0538 194 PRO B N   
3850 C  CA  . PRO B 194 ? 0.0151 0.1190 0.1319 -0.0293 0.0085  -0.0700 194 PRO B CA  
3851 C  C   . PRO B 194 ? 0.0147 0.0934 0.1266 -0.0211 -0.0033 -0.0546 194 PRO B C   
3852 O  O   . PRO B 194 ? 0.0326 0.1088 0.1106 -0.0297 -0.0008 -0.0528 194 PRO B O   
3853 C  CB  . PRO B 194 ? 0.0370 0.1399 0.1164 -0.0436 0.0131  -0.0633 194 PRO B CB  
3854 C  CG  . PRO B 194 ? 0.0458 0.1387 0.1201 -0.0425 0.0058  -0.0575 194 PRO B CG  
3855 C  CD  . PRO B 194 ? 0.0207 0.1584 0.1161 -0.0421 0.0208  -0.0687 194 PRO B CD  
3856 N  N   . GLY B 195 ? 0.0203 0.0973 0.1164 -0.0279 0.0000  -0.0622 195 GLY B N   
3857 C  CA  . GLY B 195 ? 0.0207 0.1066 0.1181 -0.0362 0.0107  -0.0571 195 GLY B CA  
3858 C  C   . GLY B 195 ? 0.0135 0.1062 0.1293 -0.0247 0.0007  -0.0442 195 GLY B C   
3859 O  O   . GLY B 195 ? 0.0143 0.1061 0.1269 -0.0281 0.0129  -0.0536 195 GLY B O   
3860 N  N   . SER B 196 ? 0.0200 0.1147 0.1186 -0.0383 0.0156  -0.0513 196 SER B N   
3861 C  CA  . SER B 196 ? 0.0126 0.1591 0.1173 -0.0299 0.0150  -0.0440 196 SER B CA  
3862 C  C   . SER B 196 ? 0.0200 0.0862 0.1353 -0.0309 0.0032  -0.0424 196 SER B C   
3863 O  O   . SER B 196 ? 0.0211 0.1177 0.1410 -0.0392 0.0144  -0.0669 196 SER B O   
3864 C  CB  . SER B 196 ? 0.0102 0.1439 0.1607 -0.0229 0.0083  -0.0658 196 SER B CB  
3865 O  OG  . SER B 196 ? 0.0184 0.1224 0.1605 -0.0367 0.0130  -0.0634 196 SER B OG  
3866 N  N   . LEU B 197 ? 0.0176 0.0953 0.1166 -0.0299 0.0093  -0.0555 197 LEU B N   
3867 C  CA  . LEU B 197 ? 0.0231 0.1187 0.1341 -0.0426 0.0183  -0.0672 197 LEU B CA  
3868 C  C   . LEU B 197 ? 0.0205 0.1106 0.1164 -0.0383 0.0211  -0.0664 197 LEU B C   
3869 O  O   . LEU B 197 ? 0.0151 0.1289 0.1322 -0.0308 0.0076  -0.0678 197 LEU B O   
3870 C  CB  . LEU B 197 ? 0.0230 0.1256 0.1375 -0.0443 0.0248  -0.0522 197 LEU B CB  
3871 C  CG  . LEU B 197 ? 0.0303 0.1421 0.1608 -0.0557 0.0089  -0.0506 197 LEU B CG  
3872 C  CD1 . LEU B 197 ? 0.0378 0.1799 0.2011 -0.0556 0.0254  -0.0328 197 LEU B CD1 
3873 C  CD2 . LEU B 197 ? 0.0211 0.2029 0.1752 -0.0250 0.0345  -0.0326 197 LEU B CD2 
3874 N  N   . THR B 198 ? 0.0173 0.1071 0.1319 -0.0327 0.0195  -0.0739 198 THR B N   
3875 C  CA  . THR B 198 ? 0.0211 0.1119 0.1590 -0.0389 0.0237  -0.0801 198 THR B CA  
3876 C  C   . THR B 198 ? 0.0238 0.1181 0.1363 -0.0428 0.0147  -0.0638 198 THR B C   
3877 O  O   . THR B 198 ? 0.0218 0.1197 0.1817 -0.0414 0.0231  -0.0826 198 THR B O   
3878 C  CB  . THR B 198 ? 0.0279 0.1020 0.1442 -0.0441 0.0160  -0.0589 198 THR B CB  
3879 O  OG1 . THR B 198 ? 0.0266 0.1068 0.1467 -0.0450 0.0240  -0.0576 198 THR B OG1 
3880 C  CG2 . THR B 198 ? 0.0232 0.0883 0.1440 -0.0369 0.0231  -0.0604 198 THR B CG2 
3881 N  N   . THR B 199 ? 0.0224 0.1076 0.1498 -0.0393 0.0133  -0.0574 199 THR B N   
3882 C  CA  . THR B 199 ? 0.0300 0.1222 0.1588 -0.0523 0.0282  -0.0598 199 THR B CA  
3883 C  C   . THR B 199 ? 0.0486 0.1464 0.1957 -0.0744 0.0548  -0.0644 199 THR B C   
3884 O  O   . THR B 199 ? 0.0447 0.1482 0.1913 -0.0736 0.0419  -0.0741 199 THR B O   
3885 C  CB  . THR B 199 ? 0.0658 0.1456 0.1821 -0.0533 -0.0212 -0.0627 199 THR B CB  
3886 O  OG1 . THR B 199 ? 0.1267 0.1787 0.2140 -0.0389 -0.0375 -0.0504 199 THR B OG1 
3887 C  CG2 . THR B 199 ? 0.1005 0.1301 0.1606 -0.0542 -0.0005 -0.0599 199 THR B CG2 
3888 N  N   . PRO B 200 ? 0.0476 0.1575 0.2171 -0.0786 0.0574  -0.0968 200 PRO B N   
3889 C  CA  . PRO B 200 ? 0.0489 0.1529 0.2248 -0.0722 0.0706  -0.0706 200 PRO B CA  
3890 C  C   . PRO B 200 ? 0.0524 0.1616 0.1927 -0.0845 0.0346  -0.0654 200 PRO B C   
3891 O  O   . PRO B 200 ? 0.0362 0.1847 0.1982 -0.0477 0.0337  -0.0469 200 PRO B O   
3892 C  CB  . PRO B 200 ? 0.0467 0.1633 0.2521 -0.0697 0.0800  -0.0815 200 PRO B CB  
3893 C  CG  . PRO B 200 ? 0.0218 0.1840 0.2278 -0.0490 0.0475  -0.1100 200 PRO B CG  
3894 C  CD  . PRO B 200 ? 0.0154 0.1855 0.2129 -0.0322 0.0386  -0.0840 200 PRO B CD  
3895 N  N   . PRO B 201 ? 0.0710 0.1509 0.1506 -0.0590 0.0239  -0.0506 201 PRO B N   
3896 C  CA  . PRO B 201 ? 0.0421 0.1486 0.1881 -0.0693 0.0267  -0.0466 201 PRO B CA  
3897 C  C   . PRO B 201 ? 0.0309 0.1551 0.1874 -0.0577 0.0142  -0.0804 201 PRO B C   
3898 O  O   . PRO B 201 ? 0.0524 0.1679 0.2129 -0.0846 0.0270  -0.0837 201 PRO B O   
3899 C  CB  . PRO B 201 ? 0.0566 0.1513 0.2097 -0.0673 0.0380  -0.0451 201 PRO B CB  
3900 C  CG  . PRO B 201 ? 0.0445 0.1289 0.2456 -0.0422 0.0464  -0.0599 201 PRO B CG  
3901 C  CD  . PRO B 201 ? 0.0798 0.1050 0.2184 -0.0707 0.0447  -0.0425 201 PRO B CD  
3902 N  N   . LEU B 202 ? 0.0242 0.1227 0.1859 -0.0422 0.0000  -0.0542 202 LEU B N   
3903 C  CA  . LEU B 202 ? 0.0245 0.1416 0.1824 -0.0478 0.0053  -0.0540 202 LEU B CA  
3904 C  C   . LEU B 202 ? 0.0419 0.1889 0.2587 -0.0794 0.0535  -0.0896 202 LEU B C   
3905 O  O   . LEU B 202 ? 0.0236 0.1588 0.2349 -0.0511 0.0222  -0.0805 202 LEU B O   
3906 C  CB  . LEU B 202 ? 0.0165 0.1522 0.2031 -0.0378 0.0067  -0.0569 202 LEU B CB  
3907 C  CG  . LEU B 202 ? 0.0106 0.1677 0.2789 -0.0206 -0.0064 -0.0961 202 LEU B CG  
3908 C  CD1 . LEU B 202 ? 0.0085 0.3764 0.3549 -0.0261 0.0188  -0.1127 202 LEU B CD1 
3909 C  CD2 . LEU B 202 ? 0.0233 0.1603 0.2590 -0.0340 -0.0151 -0.1125 202 LEU B CD2 
3910 N  N   . ALA B 203 ? 0.0372 0.1504 0.1890 -0.0666 0.0386  -0.0819 203 ALA B N   
3911 C  CA  . ALA B 203 ? 0.0328 0.1259 0.1824 -0.0556 0.0361  -0.0573 203 ALA B CA  
3912 C  C   . ALA B 203 ? 0.0336 0.0998 0.1519 -0.0494 0.0232  -0.0636 203 ALA B C   
3913 O  O   . ALA B 203 ? 0.0268 0.1020 0.1646 -0.0407 0.0075  -0.0621 203 ALA B O   
3914 C  CB  . ALA B 203 ? 0.0344 0.1183 0.1889 -0.0525 0.0288  -0.0452 203 ALA B CB  
3915 N  N   . GLU B 204 ? 0.0161 0.1364 0.1520 -0.0358 0.0177  -0.0624 204 GLU B N   
3916 C  CA  . GLU B 204 ? 0.0186 0.1257 0.1372 -0.0342 0.0067  -0.0735 204 GLU B CA  
3917 C  C   . GLU B 204 ? 0.0315 0.1179 0.1529 -0.0330 -0.0099 -0.0858 204 GLU B C   
3918 O  O   . GLU B 204 ? 0.0146 0.1539 0.1523 -0.0198 -0.0029 -0.0801 204 GLU B O   
3919 C  CB  . GLU B 204 ? 0.0245 0.1531 0.1563 -0.0233 -0.0234 -0.0879 204 GLU B CB  
3920 C  CG  . GLU B 204 ? 0.0281 0.1707 0.1938 -0.0099 -0.0418 -0.0935 204 GLU B CG  
3921 C  CD  . GLU B 204 ? 0.0368 0.1990 0.2215 -0.0565 -0.0282 -0.0763 204 GLU B CD  
3922 O  OE1 . GLU B 204 ? 0.0710 0.1786 0.2511 -0.0424 -0.0771 -0.0955 204 GLU B OE1 
3923 O  OE2 . GLU B 204 ? 0.0455 0.1812 0.2227 -0.0404 -0.0562 -0.0761 204 GLU B OE2 
3924 N  N   . CYS B 205 ? 0.0296 0.1082 0.1746 -0.0413 -0.0031 -0.0634 205 CYS B N   
3925 C  CA  . CYS B 205 ? 0.0168 0.0870 0.1467 -0.0291 0.0154  -0.0471 205 CYS B CA  
3926 C  C   . CYS B 205 ? 0.0128 0.1037 0.1204 -0.0234 0.0032  -0.0494 205 CYS B C   
3927 O  O   . CYS B 205 ? 0.0254 0.1032 0.1721 -0.0350 -0.0124 -0.0488 205 CYS B O   
3928 C  CB  . CYS B 205 ? 0.0370 0.1066 0.1637 -0.0483 -0.0022 -0.0585 205 CYS B CB  
3929 S  SG  . CYS B 205 ? 0.0456 0.1177 0.1545 -0.0419 0.0030  -0.0563 205 CYS B SG  
3930 N  N   . VAL B 206 ? 0.0135 0.0863 0.1297 -0.0220 0.0043  -0.0521 206 VAL B N   
3931 C  CA  . VAL B 206 ? 0.0209 0.0960 0.1218 -0.0352 0.0082  -0.0424 206 VAL B CA  
3932 C  C   . VAL B 206 ? 0.0184 0.0916 0.1310 -0.0320 0.0188  -0.0508 206 VAL B C   
3933 O  O   . VAL B 206 ? 0.0200 0.1193 0.1488 -0.0377 0.0232  -0.0339 206 VAL B O   
3934 C  CB  . VAL B 206 ? 0.0184 0.1032 0.1246 -0.0318 0.0045  -0.0504 206 VAL B CB  
3935 C  CG1 . VAL B 206 ? 0.0244 0.0957 0.1547 -0.0315 -0.0079 -0.0565 206 VAL B CG1 
3936 C  CG2 . VAL B 206 ? 0.0207 0.1414 0.1330 -0.0410 0.0311  -0.0566 206 VAL B CG2 
3937 N  N   . THR B 207 ? 0.0196 0.1049 0.1311 -0.0361 0.0223  -0.0593 207 THR B N   
3938 C  CA  . THR B 207 ? 0.0249 0.1034 0.1397 -0.0423 0.0312  -0.0641 207 THR B CA  
3939 C  C   . THR B 207 ? 0.0196 0.1046 0.1057 -0.0356 0.0122  -0.0501 207 THR B C   
3940 O  O   . THR B 207 ? 0.0229 0.0923 0.1155 -0.0357 0.0062  -0.0440 207 THR B O   
3941 C  CB  . THR B 207 ? 0.0195 0.1161 0.1423 -0.0377 0.0261  -0.0626 207 THR B CB  
3942 O  OG1 . THR B 207 ? 0.0176 0.1199 0.1720 -0.0354 0.0188  -0.0774 207 THR B OG1 
3943 C  CG2 . THR B 207 ? 0.0310 0.1474 0.1950 -0.0585 0.0370  -0.0716 207 THR B CG2 
3944 N  N   . TRP B 208 ? 0.0145 0.0864 0.1314 -0.0249 0.0116  -0.0557 208 TRP B N   
3945 C  CA  . TRP B 208 ? 0.0232 0.0967 0.1564 -0.0382 0.0152  -0.0566 208 TRP B CA  
3946 C  C   . TRP B 208 ? 0.0164 0.1134 0.1216 -0.0310 0.0081  -0.0600 208 TRP B C   
3947 O  O   . TRP B 208 ? 0.0183 0.1301 0.1382 -0.0328 -0.0051 -0.0531 208 TRP B O   
3948 C  CB  . TRP B 208 ? 0.0139 0.0932 0.1136 -0.0239 0.0031  -0.0441 208 TRP B CB  
3949 C  CG  . TRP B 208 ? 0.0179 0.0888 0.1172 -0.0268 0.0002  -0.0486 208 TRP B CG  
3950 C  CD1 . TRP B 208 ? 0.0225 0.0870 0.1168 -0.0256 -0.0073 -0.0539 208 TRP B CD1 
3951 C  CD2 . TRP B 208 ? 0.0200 0.0968 0.1244 -0.0343 0.0152  -0.0588 208 TRP B CD2 
3952 N  NE1 . TRP B 208 ? 0.0173 0.1240 0.1362 -0.0344 0.0070  -0.0568 208 TRP B NE1 
3953 C  CE2 . TRP B 208 ? 0.0124 0.1029 0.1291 -0.0239 0.0116  -0.0600 208 TRP B CE2 
3954 C  CE3 . TRP B 208 ? 0.0169 0.1092 0.1173 -0.0256 -0.0083 -0.0444 208 TRP B CE3 
3955 C  CZ2 . TRP B 208 ? 0.0107 0.1197 0.1436 -0.0220 0.0079  -0.0554 208 TRP B CZ2 
3956 C  CZ3 . TRP B 208 ? 0.0172 0.1088 0.1242 -0.0236 -0.0122 -0.0461 208 TRP B CZ3 
3957 C  CH2 . TRP B 208 ? 0.0139 0.1241 0.1512 -0.0278 0.0005  -0.0492 208 TRP B CH2 
3958 N  N   . ILE B 209 ? 0.0287 0.1298 0.1192 -0.0503 0.0113  -0.0585 209 ILE B N   
3959 C  CA  . ILE B 209 ? 0.0234 0.0991 0.1544 -0.0395 0.0192  -0.0558 209 ILE B CA  
3960 C  C   . ILE B 209 ? 0.0122 0.1216 0.1119 -0.0259 0.0105  -0.0548 209 ILE B C   
3961 O  O   . ILE B 209 ? 0.0223 0.0961 0.1333 -0.0367 0.0089  -0.0450 209 ILE B O   
3962 C  CB  . ILE B 209 ? 0.0218 0.0872 0.1826 -0.0323 0.0348  -0.0357 209 ILE B CB  
3963 C  CG1 . ILE B 209 ? 0.0290 0.1133 0.2188 -0.0341 -0.0048 -0.0604 209 ILE B CG1 
3964 C  CG2 . ILE B 209 ? 0.0146 0.1498 0.1929 -0.0327 0.0019  -0.0575 209 ILE B CG2 
3965 C  CD1 . ILE B 209 ? 0.0116 0.1605 0.2509 -0.0168 0.0252  -0.0502 209 ILE B CD1 
3966 N  N   . VAL B 210 ? 0.0095 0.1100 0.1539 -0.0182 0.0084  -0.0518 210 VAL B N   
3967 C  CA  . VAL B 210 ? 0.0183 0.1159 0.1230 -0.0333 -0.0010 -0.0425 210 VAL B CA  
3968 C  C   . VAL B 210 ? 0.0142 0.1091 0.1285 -0.0260 0.0015  -0.0513 210 VAL B C   
3969 O  O   . VAL B 210 ? 0.0257 0.1316 0.1464 -0.0486 0.0122  -0.0529 210 VAL B O   
3970 C  CB  . VAL B 210 ? 0.0181 0.1134 0.1928 -0.0351 0.0110  -0.0511 210 VAL B CB  
3971 C  CG1 . VAL B 210 ? 0.0300 0.1263 0.1842 -0.0526 0.0197  -0.0669 210 VAL B CG1 
3972 C  CG2 . VAL B 210 ? 0.0244 0.1116 0.2163 -0.0433 0.0203  -0.0650 210 VAL B CG2 
3973 N  N   . LEU B 211 ? 0.0243 0.1320 0.1466 -0.0440 -0.0013 -0.0460 211 LEU B N   
3974 C  CA  . LEU B 211 ? 0.0213 0.1315 0.1500 -0.0431 0.0130  -0.0528 211 LEU B CA  
3975 C  C   . LEU B 211 ? 0.0249 0.1441 0.1356 -0.0502 0.0126  -0.0516 211 LEU B C   
3976 O  O   . LEU B 211 ? 0.0276 0.1244 0.1447 -0.0480 0.0068  -0.0509 211 LEU B O   
3977 C  CB  . LEU B 211 ? 0.0249 0.1599 0.1979 -0.0414 -0.0144 -0.0724 211 LEU B CB  
3978 C  CG  . LEU B 211 ? 0.0176 0.1702 0.1951 -0.0369 -0.0136 -0.0410 211 LEU B CG  
3979 C  CD1 . LEU B 211 ? 0.0212 0.2103 0.2340 -0.0268 -0.0376 -0.0754 211 LEU B CD1 
3980 C  CD2 . LEU B 211 ? 0.0220 0.1747 0.2320 -0.0501 0.0282  -0.0534 211 LEU B CD2 
3981 N  N   . LYS B 212 ? 0.0301 0.1555 0.1645 -0.0595 0.0178  -0.0488 212 LYS B N   
3982 C  CA  . LYS B 212 ? 0.0231 0.1796 0.1658 -0.0532 0.0084  -0.0551 212 LYS B CA  
3983 C  C   . LYS B 212 ? 0.0266 0.1291 0.1621 -0.0473 -0.0052 -0.0306 212 LYS B C   
3984 O  O   . LYS B 212 ? 0.0454 0.1254 0.2316 -0.0614 -0.0266 -0.0262 212 LYS B O   
3985 C  CB  . LYS B 212 ? 0.0825 0.1835 0.1698 -0.0775 0.0226  -0.0624 212 LYS B CB  
3986 C  CG  . LYS B 212 ? 0.1502 0.2679 0.2503 -0.0845 -0.0467 0.0183  212 LYS B CG  
3987 C  CD  . LYS B 212 ? 0.3671 0.2796 0.2925 -0.1230 0.0849  -0.0726 212 LYS B CD  
3988 C  CE  . LYS B 212 ? 0.4097 0.2897 0.4934 -0.1121 0.1132  0.0416  212 LYS B CE  
3989 N  NZ  . LYS B 212 ? 0.2400 0.8338 0.5464 -0.2274 0.1374  -0.1130 212 LYS B NZ  
3990 N  N   . GLU B 213 ? 0.0290 0.1539 0.1705 -0.0542 -0.0015 -0.0500 213 GLU B N   
3991 C  CA  . GLU B 213 ? 0.0222 0.1689 0.2017 -0.0449 -0.0052 -0.0674 213 GLU B CA  
3992 C  C   . GLU B 213 ? 0.0283 0.1331 0.1772 -0.0461 -0.0061 -0.0578 213 GLU B C   
3993 O  O   . GLU B 213 ? 0.0129 0.1392 0.1987 -0.0286 -0.0013 -0.0335 213 GLU B O   
3994 C  CB  . GLU B 213 ? 0.0472 0.2903 0.2802 -0.0910 -0.0249 -0.0893 213 GLU B CB  
3995 C  CG  . GLU B 213 ? 0.1404 0.5456 0.3930 -0.2302 -0.0958 -0.0495 213 GLU B CG  
3996 C  CD  . GLU B 213 ? 0.0633 0.3576 0.6323 -0.1404 -0.0318 0.0240  213 GLU B CD  
3997 O  OE1 . GLU B 213 ? 0.0963 0.2961 0.4531 0.0006  -0.0103 0.0093  213 GLU B OE1 
3998 O  OE2 . GLU B 213 ? 0.3876 0.8090 0.5444 -0.0649 -0.0958 -0.3720 213 GLU B OE2 
3999 N  N   . PRO B 214 ? 0.0373 0.1154 0.1797 -0.0562 0.0070  -0.0471 214 PRO B N   
4000 C  CA  . PRO B 214 ? 0.0335 0.1212 0.1682 -0.0478 -0.0069 -0.0576 214 PRO B CA  
4001 C  C   . PRO B 214 ? 0.0342 0.1207 0.1761 -0.0467 -0.0165 -0.0486 214 PRO B C   
4002 O  O   . PRO B 214 ? 0.0622 0.2013 0.2549 -0.0949 -0.0375 -0.0231 214 PRO B O   
4003 C  CB  . PRO B 214 ? 0.0305 0.1318 0.2376 -0.0499 -0.0006 -0.0703 214 PRO B CB  
4004 C  CG  . PRO B 214 ? 0.0388 0.1812 0.2694 -0.0719 0.0086  -0.0813 214 PRO B CG  
4005 C  CD  . PRO B 214 ? 0.0231 0.1504 0.2125 -0.0446 0.0339  -0.0445 214 PRO B CD  
4006 N  N   . ILE B 215 ? 0.0223 0.1540 0.1593 -0.0341 -0.0166 -0.0658 215 ILE B N   
4007 C  CA  . ILE B 215 ? 0.0274 0.1430 0.1689 -0.0407 -0.0130 -0.0701 215 ILE B CA  
4008 C  C   . ILE B 215 ? 0.0208 0.1275 0.1619 -0.0374 -0.0027 -0.0542 215 ILE B C   
4009 O  O   . ILE B 215 ? 0.0290 0.1182 0.1718 -0.0218 -0.0027 -0.0554 215 ILE B O   
4010 C  CB  . ILE B 215 ? 0.0507 0.1744 0.1710 0.0108  -0.0417 -0.0713 215 ILE B CB  
4011 C  CG1 . ILE B 215 ? 0.0784 0.1228 0.1975 -0.0203 -0.0201 -0.0546 215 ILE B CG1 
4012 C  CG2 . ILE B 215 ? 0.0523 0.1932 0.1958 0.0122  -0.0250 -0.0795 215 ILE B CG2 
4013 C  CD1 . ILE B 215 ? 0.1350 0.1756 0.1963 -0.0357 -0.0309 -0.0407 215 ILE B CD1 
4014 N  N   A SER B 216 ? 0.0430 0.1177 0.1928 -0.0365 -0.0205 -0.0707 216 SER B N   
4015 N  N   B SER B 216 ? 0.0518 0.1159 0.1965 -0.0380 -0.0243 -0.0725 216 SER B N   
4016 C  CA  A SER B 216 ? 0.0547 0.1301 0.1886 -0.0414 -0.0319 -0.0773 216 SER B CA  
4017 C  CA  B SER B 216 ? 0.0631 0.1265 0.1879 -0.0414 -0.0280 -0.0745 216 SER B CA  
4018 C  C   A SER B 216 ? 0.0644 0.1258 0.1855 -0.0508 -0.0311 -0.0832 216 SER B C   
4019 C  C   B SER B 216 ? 0.0674 0.1249 0.1831 -0.0510 -0.0316 -0.0840 216 SER B C   
4020 O  O   A SER B 216 ? 0.0230 0.1733 0.1909 -0.0411 -0.0102 -0.0644 216 SER B O   
4021 O  O   B SER B 216 ? 0.0400 0.1500 0.1918 -0.0490 -0.0233 -0.0641 216 SER B O   
4022 C  CB  A SER B 216 ? 0.0875 0.1460 0.1976 -0.0715 0.0239  -0.0622 216 SER B CB  
4023 C  CB  B SER B 216 ? 0.1120 0.1681 0.1888 -0.0908 -0.0362 -0.0663 216 SER B CB  
4024 O  OG  A SER B 216 ? 0.0593 0.2558 0.2080 -0.0995 0.0122  -0.0484 216 SER B OG  
4025 O  OG  B SER B 216 ? 0.1188 0.2170 0.2478 -0.0651 -0.0314 -0.1051 216 SER B OG  
4026 N  N   . VAL B 217 ? 0.0619 0.1097 0.1680 -0.0597 -0.0193 -0.0571 217 VAL B N   
4027 C  CA  . VAL B 217 ? 0.0258 0.1295 0.1735 -0.0434 -0.0045 -0.0553 217 VAL B CA  
4028 C  C   . VAL B 217 ? 0.0396 0.1222 0.1599 -0.0494 -0.0222 -0.0440 217 VAL B C   
4029 O  O   . VAL B 217 ? 0.0439 0.1405 0.1717 -0.0469 -0.0251 -0.0490 217 VAL B O   
4030 C  CB  . VAL B 217 ? 0.0465 0.1053 0.2195 -0.0553 -0.0004 -0.0687 217 VAL B CB  
4031 C  CG1 . VAL B 217 ? 0.1075 0.1094 0.2061 -0.0697 -0.0359 -0.0766 217 VAL B CG1 
4032 C  CG2 . VAL B 217 ? 0.0484 0.1560 0.2355 -0.0628 -0.0176 -0.0499 217 VAL B CG2 
4033 N  N   . SER B 218 ? 0.0697 0.1087 0.1508 -0.0582 -0.0157 -0.0545 218 SER B N   
4034 C  CA  . SER B 218 ? 0.0797 0.1133 0.1857 -0.0441 -0.0381 -0.0675 218 SER B CA  
4035 C  C   . SER B 218 ? 0.0877 0.1100 0.1567 -0.0577 -0.0286 -0.0684 218 SER B C   
4036 O  O   . SER B 218 ? 0.0755 0.1019 0.1909 -0.0495 -0.0315 -0.0615 218 SER B O   
4037 C  CB  . SER B 218 ? 0.0815 0.1852 0.1720 -0.0497 -0.0323 -0.0417 218 SER B CB  
4038 O  OG  . SER B 218 ? 0.1366 0.1314 0.1767 -0.0595 -0.0446 -0.0582 218 SER B OG  
4039 N  N   A SER B 219 ? 0.0615 0.1191 0.2006 -0.0476 -0.0163 -0.0770 219 SER B N   
4040 N  N   B SER B 219 ? 0.1383 0.1148 0.1960 -0.0488 -0.0399 -0.0855 219 SER B N   
4041 C  CA  A SER B 219 ? 0.0604 0.1217 0.2261 -0.0725 -0.0020 -0.0602 219 SER B CA  
4042 C  CA  B SER B 219 ? 0.1342 0.0930 0.2253 -0.0886 -0.0158 -0.0631 219 SER B CA  
4043 C  C   A SER B 219 ? 0.1124 0.0957 0.2225 -0.0796 0.0182  -0.0587 219 SER B C   
4044 C  C   B SER B 219 ? 0.1678 0.1014 0.2150 -0.0648 0.0021  -0.0576 219 SER B C   
4045 O  O   A SER B 219 ? 0.0872 0.1409 0.2229 -0.0701 0.0013  -0.0604 219 SER B O   
4046 O  O   B SER B 219 ? 0.1490 0.1363 0.2243 -0.0648 0.0022  -0.0757 219 SER B O   
4047 C  CB  A SER B 219 ? 0.0736 0.1165 0.2310 -0.0602 0.0253  -0.0769 219 SER B CB  
4048 C  CB  B SER B 219 ? 0.1775 0.0991 0.2692 -0.0592 -0.0132 -0.0692 219 SER B CB  
4049 O  OG  A SER B 219 ? 0.1130 0.1316 0.2003 -0.0218 -0.0234 -0.0395 219 SER B OG  
4050 O  OG  B SER B 219 ? 0.2133 0.1681 0.2572 -0.0232 0.0208  -0.0597 219 SER B OG  
4051 N  N   . GLU B 220 ? 0.1505 0.1097 0.2008 -0.0431 0.0089  -0.0597 220 GLU B N   
4052 C  CA  . GLU B 220 ? 0.1383 0.1396 0.1812 -0.0788 -0.0084 -0.0730 220 GLU B CA  
4053 C  C   . GLU B 220 ? 0.1103 0.1444 0.1867 -0.0723 0.0027  -0.0582 220 GLU B C   
4054 O  O   . GLU B 220 ? 0.1884 0.1736 0.1756 -0.0610 0.0364  -0.0641 220 GLU B O   
4055 C  CB  . GLU B 220 ? 0.2190 0.1889 0.2428 -0.1226 -0.0813 -0.1010 220 GLU B CB  
4056 C  CG  . GLU B 220 ? 0.4055 0.1754 0.2707 -0.0964 -0.0933 -0.0800 220 GLU B CG  
4057 C  CD  . GLU B 220 ? 0.3930 0.1419 0.3449 -0.1355 -0.0262 -0.1328 220 GLU B CD  
4058 O  OE1 . GLU B 220 ? 0.3052 0.2048 0.3105 -0.1514 0.0428  -0.1180 220 GLU B OE1 
4059 O  OE2 . GLU B 220 ? 0.6822 0.1897 0.4448 -0.2423 0.0479  -0.1870 220 GLU B OE2 
4060 N  N   . GLN B 221 ? 0.1059 0.1150 0.1779 -0.0658 -0.0258 -0.0569 221 GLN B N   
4061 C  CA  . GLN B 221 ? 0.1106 0.1116 0.1793 -0.0908 -0.0165 -0.0440 221 GLN B CA  
4062 C  C   . GLN B 221 ? 0.0751 0.1301 0.1839 -0.0558 0.0020  -0.0564 221 GLN B C   
4063 O  O   . GLN B 221 ? 0.1211 0.1354 0.1804 -0.0779 -0.0020 -0.0389 221 GLN B O   
4064 C  CB  . GLN B 221 ? 0.1220 0.1487 0.1601 -0.0614 -0.0414 -0.0466 221 GLN B CB  
4065 C  CG  . GLN B 221 ? 0.1283 0.1315 0.1739 -0.0655 -0.0636 -0.0727 221 GLN B CG  
4066 C  CD  . GLN B 221 ? 0.1134 0.1252 0.1890 -0.0882 -0.0419 -0.0480 221 GLN B CD  
4067 O  OE1 . GLN B 221 ? 0.0885 0.1213 0.1784 -0.0443 -0.0401 -0.0554 221 GLN B OE1 
4068 N  NE2 . GLN B 221 ? 0.1597 0.1333 0.1922 -0.0530 -0.0603 -0.0534 221 GLN B NE2 
4069 N  N   A VAL B 222 ? 0.1212 0.1209 0.1780 -0.0937 -0.0296 -0.0480 222 VAL B N   
4070 N  N   B VAL B 222 ? 0.1230 0.1274 0.1850 -0.0885 -0.0206 -0.0406 222 VAL B N   
4071 C  CA  A VAL B 222 ? 0.0951 0.1128 0.1698 -0.0820 -0.0030 -0.0491 222 VAL B CA  
4072 C  CA  B VAL B 222 ? 0.0940 0.1603 0.1922 -0.0738 0.0076  -0.0455 222 VAL B CA  
4073 C  C   A VAL B 222 ? 0.1475 0.1288 0.1870 -0.0823 0.0301  -0.0520 222 VAL B C   
4074 C  C   B VAL B 222 ? 0.1591 0.1358 0.1866 -0.0792 0.0305  -0.0569 222 VAL B C   
4075 O  O   A VAL B 222 ? 0.1351 0.1379 0.1989 -0.0740 -0.0024 -0.0442 222 VAL B O   
4076 O  O   B VAL B 222 ? 0.1491 0.1484 0.1619 -0.0700 0.0403  -0.0341 222 VAL B O   
4077 C  CB  A VAL B 222 ? 0.0750 0.1710 0.1834 -0.0642 -0.0047 -0.0158 222 VAL B CB  
4078 C  CB  B VAL B 222 ? 0.1200 0.2425 0.1965 -0.0455 0.0436  -0.0150 222 VAL B CB  
4079 C  CG1 A VAL B 222 ? 0.0333 0.1794 0.2288 -0.0649 -0.0226 -0.0052 222 VAL B CG1 
4080 C  CG1 B VAL B 222 ? 0.1499 0.3070 0.2940 0.0194  -0.0115 -0.0001 222 VAL B CG1 
4081 C  CG2 A VAL B 222 ? 0.0737 0.1500 0.1861 -0.0444 -0.0124 -0.0289 222 VAL B CG2 
4082 C  CG2 B VAL B 222 ? 0.0370 0.3071 0.2812 -0.0373 0.0828  0.0130  222 VAL B CG2 
4083 N  N   . LEU B 223 ? 0.1554 0.1118 0.1901 -0.0590 0.0218  -0.0516 223 LEU B N   
4084 C  CA  . LEU B 223 ? 0.1747 0.1249 0.2308 -0.0232 0.0339  -0.0440 223 LEU B CA  
4085 C  C   . LEU B 223 ? 0.1138 0.1503 0.1744 -0.0670 0.0309  -0.0598 223 LEU B C   
4086 O  O   . LEU B 223 ? 0.1202 0.1907 0.2185 -0.0908 0.0285  -0.0608 223 LEU B O   
4087 C  CB  . LEU B 223 ? 0.2118 0.1854 0.2759 -0.0925 0.0635  -0.0825 223 LEU B CB  
4088 C  CG  . LEU B 223 ? 0.3753 0.2128 0.3641 -0.1192 0.0103  -0.0387 223 LEU B CG  
4089 C  CD1 . LEU B 223 ? 0.3221 0.3222 0.5066 -0.1166 -0.1296 -0.0763 223 LEU B CD1 
4090 C  CD2 . LEU B 223 ? 0.4504 0.2296 0.4359 -0.0262 -0.1127 -0.2159 223 LEU B CD2 
4091 N  N   . LYS B 224 ? 0.1195 0.1484 0.1927 -0.0844 0.0219  -0.0721 224 LYS B N   
4092 C  CA  . LYS B 224 ? 0.1779 0.2092 0.1971 -0.1204 0.0414  -0.0370 224 LYS B CA  
4093 C  C   . LYS B 224 ? 0.1322 0.1650 0.1609 -0.0515 0.0179  -0.0305 224 LYS B C   
4094 O  O   . LYS B 224 ? 0.1889 0.1710 0.1495 -0.1047 0.0117  -0.0337 224 LYS B O   
4095 C  CB  . LYS B 224 ? 0.3087 0.3596 0.2345 -0.1065 -0.1188 0.0129  224 LYS B CB  
4096 C  CG  . LYS B 224 ? 0.3565 0.3563 0.2350 -0.1253 -0.0833 0.0025  224 LYS B CG  
4097 C  CD  . LYS B 224 ? 0.4237 0.6589 0.3304 -0.1525 -0.1394 0.0111  224 LYS B CD  
4098 C  CE  . LYS B 224 ? 0.6088 0.7629 0.3328 -0.1016 -0.1874 -0.0080 224 LYS B CE  
4099 N  NZ  . LYS B 224 ? 0.4203 0.7464 0.6177 -0.2361 -0.0605 0.2082  224 LYS B NZ  
4100 N  N   . PHE B 225 ? 0.1538 0.1146 0.1400 -0.0514 0.0184  -0.0450 225 PHE B N   
4101 C  CA  . PHE B 225 ? 0.1348 0.1140 0.1630 -0.0680 0.0420  -0.0547 225 PHE B CA  
4102 C  C   . PHE B 225 ? 0.1507 0.1035 0.1393 -0.0670 0.0367  -0.0573 225 PHE B C   
4103 O  O   . PHE B 225 ? 0.1540 0.1612 0.1457 -0.0904 0.0388  -0.0471 225 PHE B O   
4104 C  CB  . PHE B 225 ? 0.1548 0.1314 0.1583 -0.0411 0.0323  -0.0691 225 PHE B CB  
4105 C  CG  . PHE B 225 ? 0.1079 0.0974 0.1811 -0.0671 -0.0022 -0.0776 225 PHE B CG  
4106 C  CD1 . PHE B 225 ? 0.1722 0.1448 0.1972 -0.0315 0.0111  -0.0454 225 PHE B CD1 
4107 C  CD2 . PHE B 225 ? 0.0723 0.1892 0.1844 -0.0575 0.0030  -0.0752 225 PHE B CD2 
4108 C  CE1 . PHE B 225 ? 0.2260 0.1336 0.2347 -0.0201 0.0440  -0.0334 225 PHE B CE1 
4109 C  CE2 . PHE B 225 ? 0.0491 0.2164 0.2039 -0.0671 0.0038  -0.0974 225 PHE B CE2 
4110 C  CZ  . PHE B 225 ? 0.1302 0.1479 0.2397 -0.0234 0.0203  -0.0842 225 PHE B CZ  
4111 N  N   . ARG B 226 ? 0.1330 0.1176 0.1401 -0.0456 0.0219  -0.0551 226 ARG B N   
4112 C  CA  . ARG B 226 ? 0.1243 0.1361 0.1497 -0.0643 0.0111  -0.0548 226 ARG B CA  
4113 C  C   . ARG B 226 ? 0.1302 0.1105 0.1610 -0.0920 0.0162  -0.0467 226 ARG B C   
4114 O  O   . ARG B 226 ? 0.1417 0.1635 0.1655 -0.0796 0.0332  -0.0697 226 ARG B O   
4115 C  CB  . ARG B 226 ? 0.0933 0.1578 0.1698 -0.0636 0.0260  -0.0412 226 ARG B CB  
4116 C  CG  . ARG B 226 ? 0.1147 0.1602 0.1539 -0.0920 0.0313  -0.0697 226 ARG B CG  
4117 C  CD  . ARG B 226 ? 0.2358 0.1771 0.1846 -0.0141 0.0521  -0.0201 226 ARG B CD  
4118 N  NE  . ARG B 226 ? 0.1312 0.1545 0.1614 -0.0928 0.0093  -0.0527 226 ARG B NE  
4119 C  CZ  . ARG B 226 ? 0.1368 0.1523 0.1575 -0.1075 -0.0023 -0.0626 226 ARG B CZ  
4120 N  NH1 . ARG B 226 ? 0.1588 0.1964 0.2124 -0.1389 0.0051  -0.1012 226 ARG B NH1 
4121 N  NH2 . ARG B 226 ? 0.1727 0.1617 0.1727 -0.0929 0.0374  -0.0495 226 ARG B NH2 
4122 N  N   . LYS B 227 ? 0.1474 0.1168 0.1532 -0.0783 0.0254  -0.0651 227 LYS B N   
4123 C  CA  . LYS B 227 ? 0.2190 0.1378 0.1582 -0.1231 0.0392  -0.0917 227 LYS B CA  
4124 C  C   . LYS B 227 ? 0.2130 0.1399 0.1374 -0.1183 0.0159  -0.0721 227 LYS B C   
4125 O  O   . LYS B 227 ? 0.2264 0.2100 0.1430 -0.1319 0.0289  -0.0714 227 LYS B O   
4126 C  CB  . LYS B 227 ? 0.2633 0.1879 0.1515 -0.1507 0.0059  -0.0605 227 LYS B CB  
4127 C  CG  . LYS B 227 ? 0.3174 0.2204 0.2581 -0.1527 0.0240  -0.1236 227 LYS B CG  
4128 C  CD  . LYS B 227 ? 0.2854 0.3726 0.3255 -0.1879 0.0174  -0.1427 227 LYS B CD  
4129 C  CE  . LYS B 227 ? 0.5164 0.6121 0.3701 -0.2730 0.1921  -0.0691 227 LYS B CE  
4130 N  NZ  . LYS B 227 ? 0.7100 0.8176 0.5715 -0.4593 -0.0889 -0.0210 227 LYS B NZ  
4131 N  N   . LEU B 228 ? 0.1670 0.1331 0.1518 -0.1187 -0.0016 -0.0724 228 LEU B N   
4132 C  CA  . LEU B 228 ? 0.2079 0.2116 0.1645 -0.1754 -0.0087 -0.0835 228 LEU B CA  
4133 C  C   . LEU B 228 ? 0.2312 0.1757 0.1271 -0.1561 0.0200  -0.0577 228 LEU B C   
4134 O  O   . LEU B 228 ? 0.2100 0.1586 0.1522 -0.1315 0.0356  -0.0688 228 LEU B O   
4135 C  CB  . LEU B 228 ? 0.2425 0.1371 0.1530 -0.1297 0.0016  -0.0591 228 LEU B CB  
4136 C  CG  . LEU B 228 ? 0.1578 0.2335 0.1304 -0.1336 0.0066  -0.0409 228 LEU B CG  
4137 C  CD1 . LEU B 228 ? 0.1861 0.1523 0.1859 -0.1064 -0.0073 -0.0829 228 LEU B CD1 
4138 C  CD2 . LEU B 228 ? 0.2849 0.1937 0.1588 -0.0802 0.0055  -0.0588 228 LEU B CD2 
4139 N  N   . ASN B 229 ? 0.2579 0.2329 0.1451 -0.2120 0.0414  -0.0662 229 ASN B N   
4140 C  CA  . ASN B 229 ? 0.2990 0.2001 0.1462 -0.1793 0.0730  -0.0643 229 ASN B CA  
4141 C  C   . ASN B 229 ? 0.3304 0.1932 0.1592 -0.1725 0.0972  -0.0787 229 ASN B C   
4142 O  O   . ASN B 229 ? 0.2086 0.2258 0.1911 -0.1892 0.0532  -0.0663 229 ASN B O   
4143 C  CB  . ASN B 229 ? 0.3649 0.2901 0.1604 -0.2144 0.1043  -0.0987 229 ASN B CB  
4144 C  CG  . ASN B 229 ? 0.4497 0.2636 0.1649 -0.2495 0.0860  -0.0937 229 ASN B CG  
4145 O  OD1 . ASN B 229 ? 0.5446 0.3646 0.1930 -0.2384 0.1419  -0.1101 229 ASN B OD1 
4146 N  ND2 . ASN B 229 ? 0.3942 0.2440 0.1884 -0.1932 0.1368  -0.1029 229 ASN B ND2 
4147 N  N   . PHE B 230 ? 0.2859 0.2649 0.1408 -0.2264 0.0872  -0.0884 230 PHE B N   
4148 C  CA  . PHE B 230 ? 0.2606 0.2102 0.1614 -0.1932 0.1030  -0.0952 230 PHE B CA  
4149 C  C   . PHE B 230 ? 0.2946 0.2533 0.1747 -0.2102 0.0759  -0.0509 230 PHE B C   
4150 O  O   . PHE B 230 ? 0.2760 0.2631 0.1845 -0.2167 0.0822  -0.0930 230 PHE B O   
4151 C  CB  . PHE B 230 ? 0.2646 0.2745 0.1761 -0.2257 0.0879  -0.0853 230 PHE B CB  
4152 C  CG  . PHE B 230 ? 0.2147 0.2416 0.1764 -0.1760 0.1054  -0.0908 230 PHE B CG  
4153 C  CD1 . PHE B 230 ? 0.1947 0.2319 0.1521 -0.1451 0.0484  -0.0876 230 PHE B CD1 
4154 C  CD2 . PHE B 230 ? 0.2185 0.2275 0.2023 -0.1989 0.0598  -0.0605 230 PHE B CD2 
4155 C  CE1 . PHE B 230 ? 0.1721 0.2818 0.1556 -0.1482 0.0581  -0.0788 230 PHE B CE1 
4156 C  CE2 . PHE B 230 ? 0.2194 0.2314 0.1759 -0.1819 0.0752  -0.1007 230 PHE B CE2 
4157 C  CZ  . PHE B 230 ? 0.1942 0.2546 0.2111 -0.2097 0.0652  -0.1236 230 PHE B CZ  
4158 N  N   . ASN B 231 ? 0.3057 0.2652 0.1841 -0.2213 0.1172  -0.0901 231 ASN B N   
4159 C  CA  . ASN B 231 ? 0.2509 0.2912 0.1992 -0.2300 0.0868  -0.0815 231 ASN B CA  
4160 C  C   . ASN B 231 ? 0.2483 0.2309 0.2004 -0.0950 0.1356  -0.0959 231 ASN B C   
4161 O  O   . ASN B 231 ? 0.3158 0.2258 0.2213 -0.1344 0.1252  -0.0659 231 ASN B O   
4162 C  CB  . ASN B 231 ? 0.3887 0.2497 0.2467 -0.2491 0.1415  -0.0936 231 ASN B CB  
4163 C  CG  . ASN B 231 ? 0.2935 0.2643 0.2313 -0.1848 0.0510  -0.0547 231 ASN B CG  
4164 O  OD1 . ASN B 231 ? 0.4316 0.3046 0.2294 -0.2445 0.1622  -0.1141 231 ASN B OD1 
4165 N  ND2 . ASN B 231 ? 0.3994 0.2237 0.2206 -0.1711 0.0790  -0.0650 231 ASN B ND2 
4166 N  N   . GLY B 232 ? 0.4438 0.2457 0.2672 -0.1826 0.1481  -0.0575 232 GLY B N   
4167 C  CA  . GLY B 232 ? 0.3314 0.2767 0.2973 -0.1573 0.1094  -0.0615 232 GLY B CA  
4168 C  C   . GLY B 232 ? 0.1278 0.1964 0.3168 -0.0484 -0.0396 -0.0004 232 GLY B C   
4169 O  O   . GLY B 232 ? 0.1963 0.2569 0.3306 0.0217  0.1588  -0.0633 232 GLY B O   
4170 N  N   . GLU B 233 ? 0.1618 0.2874 0.2131 -0.0754 0.0107  -0.0073 233 GLU B N   
4171 C  CA  . GLU B 233 ? 0.0834 0.2120 0.2691 -0.1120 -0.0233 -0.0134 233 GLU B CA  
4172 C  C   . GLU B 233 ? 0.2349 0.3630 0.3838 -0.0182 0.0556  -0.1149 233 GLU B C   
4173 O  O   . GLU B 233 ? 0.5721 0.3765 0.3277 -0.0100 0.1526  -0.1385 233 GLU B O   
4174 C  CB  . GLU B 233 ? 0.1594 0.2388 0.2500 0.0098  -0.0019 -0.0695 233 GLU B CB  
4175 C  CG  . GLU B 233 ? 0.0714 0.3662 0.2177 -0.0621 0.0472  -0.0332 233 GLU B CG  
4176 C  CD  . GLU B 233 ? 0.3661 0.3955 0.2583 -0.0247 -0.0167 -0.0824 233 GLU B CD  
4177 O  OE1 . GLU B 233 ? 0.3583 0.3298 0.4092 -0.1486 0.2017  -0.0685 233 GLU B OE1 
4178 O  OE2 . GLU B 233 ? 0.5046 0.5233 0.3286 -0.1419 -0.0772 -0.1377 233 GLU B OE2 
4179 N  N   . GLY B 234 ? 0.3955 0.6296 0.4338 0.0050  0.0732  -0.1035 234 GLY B N   
4180 C  CA  . GLY B 234 ? 0.2715 0.7030 0.4388 -0.1268 0.1361  -0.2287 234 GLY B CA  
4181 C  C   . GLY B 234 ? 0.7755 0.4181 0.4561 -0.0554 0.1395  -0.1588 234 GLY B C   
4182 O  O   . GLY B 234 ? 0.9230 0.3416 0.3559 -0.2464 0.3319  -0.1597 234 GLY B O   
4183 N  N   . GLU B 235 ? 0.8408 0.2396 0.3588 -0.2992 0.2240  -0.1314 235 GLU B N   
4184 C  CA  . GLU B 235 ? 0.6514 0.3036 0.5999 -0.2974 0.2384  -0.0478 235 GLU B CA  
4185 C  C   . GLU B 235 ? 0.3904 0.1799 0.2062 0.0697  0.0978  -0.0436 235 GLU B C   
4186 O  O   . GLU B 235 ? 0.4906 0.4942 0.3265 -0.1777 0.2022  -0.0987 235 GLU B O   
4187 C  CB  . GLU B 235 ? 0.8604 0.5576 0.6114 -0.3346 0.1251  -0.1106 235 GLU B CB  
4188 C  CG  . GLU B 235 ? 0.9054 0.4568 1.0117 -0.3784 -0.0985 -0.2396 235 GLU B CG  
4189 C  CD  . GLU B 235 ? 0.9182 1.0730 1.1348 -0.3006 -0.1238 -0.0177 235 GLU B CD  
4190 O  OE1 . GLU B 235 ? 0.7154 1.3467 1.0898 0.0298  -0.0793 -0.0638 235 GLU B OE1 
4191 O  OE2 . GLU B 235 ? 1.0750 1.2237 1.3489 -0.3987 -0.2505 0.1694  235 GLU B OE2 
4192 N  N   . PRO B 236 ? 0.1298 0.3236 0.3416 0.0125  0.0546  -0.0642 236 PRO B N   
4193 C  CA  . PRO B 236 ? 0.3476 0.3438 0.2264 -0.0522 0.0901  -0.0069 236 PRO B CA  
4194 C  C   . PRO B 236 ? 0.4559 0.3691 0.2356 -0.2752 0.1472  -0.1492 236 PRO B C   
4195 O  O   . PRO B 236 ? 0.4646 0.4873 0.3174 -0.1382 0.1868  -0.2355 236 PRO B O   
4196 C  CB  . PRO B 236 ? 0.2148 0.2994 0.3501 -0.0800 0.1283  -0.0303 236 PRO B CB  
4197 C  CG  . PRO B 236 ? 0.1439 0.2424 0.3890 -0.0025 0.1351  -0.0787 236 PRO B CG  
4198 C  CD  . PRO B 236 ? 0.1127 0.2744 0.4283 0.0392  0.0969  0.0127  236 PRO B CD  
4199 N  N   . GLU B 237 ? 0.3218 0.4327 0.1945 -0.2684 0.0890  -0.1151 237 GLU B N   
4200 C  CA  . GLU B 237 ? 0.3590 0.3653 0.2477 -0.1921 0.0910  -0.0590 237 GLU B CA  
4201 C  C   . GLU B 237 ? 0.3608 0.3703 0.2215 -0.1061 0.1163  -0.0743 237 GLU B C   
4202 O  O   . GLU B 237 ? 0.1878 0.4385 0.2230 -0.1410 0.0788  -0.0936 237 GLU B O   
4203 C  CB  . GLU B 237 ? 0.4409 0.5957 0.2274 -0.1085 -0.0040 0.0800  237 GLU B CB  
4204 C  CG  . GLU B 237 ? 0.5022 0.4086 0.3749 -0.0342 0.0252  -0.0518 237 GLU B CG  
4205 C  CD  . GLU B 237 ? 0.7102 0.5417 0.3233 -0.1224 -0.0257 -0.0223 237 GLU B CD  
4206 O  OE1 . GLU B 237 ? 0.1709 0.7938 0.3625 -0.0392 -0.0421 -0.1251 237 GLU B OE1 
4207 O  OE2 . GLU B 237 ? 0.6447 0.5940 0.4642 0.0077  0.0304  -0.1303 237 GLU B OE2 
4208 N  N   A GLU B 238 ? 0.1864 0.4613 0.2448 -0.2367 0.0482  -0.1974 238 GLU B N   
4209 N  N   B GLU B 238 ? 0.2867 0.3325 0.1756 -0.2420 0.1292  -0.0994 238 GLU B N   
4210 C  CA  A GLU B 238 ? 0.1288 0.4141 0.3110 -0.2160 0.0310  -0.1181 238 GLU B CA  
4211 C  CA  B GLU B 238 ? 0.1702 0.3527 0.1659 -0.2137 0.0388  -0.1298 238 GLU B CA  
4212 C  C   A GLU B 238 ? 0.1687 0.3790 0.1648 -0.2105 0.0496  -0.0908 238 GLU B C   
4213 C  C   B GLU B 238 ? 0.2058 0.3851 0.2145 -0.2049 0.0331  -0.0822 238 GLU B C   
4214 O  O   A GLU B 238 ? 0.3349 0.3790 0.1495 -0.0851 0.0416  -0.0724 238 GLU B O   
4215 O  O   B GLU B 238 ? 0.5211 0.3587 0.2182 -0.1183 0.0402  -0.0750 238 GLU B O   
4216 C  CB  A GLU B 238 ? 0.0106 0.5134 0.3255 -0.0089 -0.0313 -0.1417 238 GLU B CB  
4217 C  CB  B GLU B 238 ? 0.2653 0.3378 0.2645 -0.2225 0.0525  -0.1508 238 GLU B CB  
4218 C  CG  A GLU B 238 ? 0.0147 0.4233 0.2594 -0.0551 0.0072  -0.1628 238 GLU B CG  
4219 C  CG  B GLU B 238 ? 0.1096 0.5623 0.2856 -0.0443 -0.0229 -0.1955 238 GLU B CG  
4220 C  CD  A GLU B 238 ? 0.1673 0.4018 0.1849 -0.1599 -0.0275 -0.1729 238 GLU B CD  
4221 C  CD  B GLU B 238 ? 0.0372 0.6444 0.4355 0.1101  -0.0682 -0.2103 238 GLU B CD  
4222 O  OE1 A GLU B 238 ? 0.2135 0.4330 0.2105 -0.1072 0.0067  -0.1390 238 GLU B OE1 
4223 O  OE1 B GLU B 238 ? 0.1922 0.5389 0.4318 0.0211  -0.1134 -0.1277 238 GLU B OE1 
4224 O  OE2 A GLU B 238 ? 0.2378 0.7522 0.2918 -0.3741 -0.0264 -0.1570 238 GLU B OE2 
4225 O  OE2 B GLU B 238 ? 0.1980 0.4379 0.4329 -0.0846 0.0383  -0.0100 238 GLU B OE2 
4226 N  N   A LEU B 239 ? 0.1733 0.2456 0.1674 -0.1821 0.0763  -0.0834 239 LEU B N   
4227 N  N   B LEU B 239 ? 0.1682 0.2687 0.1769 -0.1711 0.0745  -0.0900 239 LEU B N   
4228 C  CA  A LEU B 239 ? 0.1584 0.1843 0.1612 -0.1112 0.0739  -0.0839 239 LEU B CA  
4229 C  CA  B LEU B 239 ? 0.1536 0.1803 0.1755 -0.1394 0.0858  -0.0936 239 LEU B CA  
4230 C  C   A LEU B 239 ? 0.1411 0.1540 0.1419 -0.1241 0.0508  -0.0644 239 LEU B C   
4231 C  C   B LEU B 239 ? 0.1365 0.1671 0.1417 -0.1225 0.0540  -0.0636 239 LEU B C   
4232 O  O   A LEU B 239 ? 0.1404 0.1961 0.1805 -0.1453 0.0566  -0.0302 239 LEU B O   
4233 O  O   B LEU B 239 ? 0.0985 0.2721 0.1303 -0.1248 0.0886  -0.1075 239 LEU B O   
4234 C  CB  A LEU B 239 ? 0.1140 0.1502 0.1875 -0.0726 0.0247  -0.0785 239 LEU B CB  
4235 C  CB  B LEU B 239 ? 0.1238 0.1987 0.2047 -0.1462 0.0883  -0.0735 239 LEU B CB  
4236 C  CG  A LEU B 239 ? 0.0766 0.1545 0.1858 -0.0475 -0.0168 -0.0797 239 LEU B CG  
4237 C  CG  B LEU B 239 ? 0.0852 0.1749 0.1925 -0.0974 0.0813  -0.0677 239 LEU B CG  
4238 C  CD1 A LEU B 239 ? 0.0363 0.1709 0.3626 -0.0522 0.0055  -0.0785 239 LEU B CD1 
4239 C  CD1 B LEU B 239 ? 0.0600 0.1228 0.2446 -0.0111 0.0318  -0.0606 239 LEU B CD1 
4240 C  CD2 A LEU B 239 ? 0.0243 0.1174 0.1091 -0.0445 0.0354  -0.0929 239 LEU B CD2 
4241 C  CD2 B LEU B 239 ? 0.1048 0.0973 0.2423 -0.0749 0.0428  -0.0767 239 LEU B CD2 
4242 N  N   . MET B 240 ? 0.1199 0.1781 0.1467 -0.0985 0.0512  -0.0618 240 MET B N   
4243 C  CA  . MET B 240 ? 0.1474 0.1632 0.1313 -0.1093 0.0657  -0.0480 240 MET B CA  
4244 C  C   . MET B 240 ? 0.1043 0.1531 0.1402 -0.1198 0.0685  -0.0800 240 MET B C   
4245 O  O   . MET B 240 ? 0.0875 0.1634 0.1390 -0.0867 0.0383  -0.0562 240 MET B O   
4246 C  CB  . MET B 240 ? 0.2017 0.1947 0.1313 -0.1004 0.0443  -0.0717 240 MET B CB  
4247 C  CG  . MET B 240 ? 0.1556 0.2007 0.1467 -0.1338 0.0677  -0.0778 240 MET B CG  
4248 S  SD  . MET B 240 ? 0.2291 0.1471 0.1690 -0.1286 0.0431  -0.0586 240 MET B SD  
4249 C  CE  . MET B 240 ? 0.2355 0.1958 0.1545 -0.1582 0.0646  -0.0820 240 MET B CE  
4250 N  N   . VAL B 241 ? 0.1127 0.1333 0.1331 -0.0966 0.0633  -0.0686 241 VAL B N   
4251 C  CA  . VAL B 241 ? 0.1233 0.1246 0.1195 -0.0466 0.0497  -0.0578 241 VAL B CA  
4252 C  C   . VAL B 241 ? 0.0429 0.1443 0.1464 -0.0650 0.0528  -0.0577 241 VAL B C   
4253 O  O   . VAL B 241 ? 0.0465 0.1599 0.1505 -0.0765 0.0491  -0.0724 241 VAL B O   
4254 C  CB  . VAL B 241 ? 0.0633 0.1355 0.1650 -0.0835 0.0454  -0.0944 241 VAL B CB  
4255 C  CG1 . VAL B 241 ? 0.0608 0.1857 0.1632 -0.0957 0.0378  -0.0757 241 VAL B CG1 
4256 C  CG2 . VAL B 241 ? 0.0981 0.1336 0.1869 -0.0693 0.0784  -0.0729 241 VAL B CG2 
4257 N  N   . ASP B 242 ? 0.0475 0.1182 0.1346 -0.0674 0.0360  -0.0701 242 ASP B N   
4258 C  CA  . ASP B 242 ? 0.0710 0.1010 0.1296 -0.0257 0.0316  -0.0716 242 ASP B CA  
4259 C  C   . ASP B 242 ? 0.0387 0.1172 0.1294 -0.0579 0.0336  -0.0602 242 ASP B C   
4260 O  O   . ASP B 242 ? 0.0384 0.1426 0.1777 -0.0494 0.0194  -0.0818 242 ASP B O   
4261 C  CB  . ASP B 242 ? 0.0457 0.1076 0.1439 -0.0524 0.0269  -0.0624 242 ASP B CB  
4262 C  CG  . ASP B 242 ? 0.0335 0.1064 0.1546 -0.0447 0.0374  -0.0622 242 ASP B CG  
4263 O  OD1 . ASP B 242 ? 0.0310 0.1158 0.1676 -0.0516 0.0284  -0.0721 242 ASP B OD1 
4264 O  OD2 . ASP B 242 ? 0.0498 0.1183 0.1832 -0.0441 0.0316  -0.0834 242 ASP B OD2 
4265 N  N   . ASN B 243 ? 0.0416 0.0973 0.1249 -0.0557 0.0378  -0.0586 243 ASN B N   
4266 C  CA  . ASN B 243 ? 0.0535 0.1209 0.1437 -0.0726 0.0521  -0.0660 243 ASN B CA  
4267 C  C   . ASN B 243 ? 0.0387 0.1256 0.1494 -0.0616 0.0341  -0.0787 243 ASN B C   
4268 O  O   . ASN B 243 ? 0.0520 0.1182 0.1326 -0.0606 0.0309  -0.0622 243 ASN B O   
4269 C  CB  . ASN B 243 ? 0.0726 0.1499 0.1429 -0.0971 0.0570  -0.0742 243 ASN B CB  
4270 C  CG  . ASN B 243 ? 0.0786 0.1295 0.1458 -0.0931 0.0462  -0.0776 243 ASN B CG  
4271 O  OD1 . ASN B 243 ? 0.0549 0.1259 0.1741 -0.0761 0.0268  -0.0404 243 ASN B OD1 
4272 N  ND2 . ASN B 243 ? 0.0933 0.1509 0.1675 -0.1023 -0.0060 -0.0511 243 ASN B ND2 
4273 N  N   . TRP B 244 ? 0.0400 0.1336 0.1346 -0.0647 0.0292  -0.0728 244 TRP B N   
4274 C  CA  . TRP B 244 ? 0.0300 0.1128 0.1279 -0.0501 0.0306  -0.0717 244 TRP B CA  
4275 C  C   . TRP B 244 ? 0.0254 0.1110 0.1500 -0.0441 0.0218  -0.0691 244 TRP B C   
4276 O  O   . TRP B 244 ? 0.0263 0.1188 0.1509 -0.0234 0.0176  -0.0542 244 TRP B O   
4277 C  CB  . TRP B 244 ? 0.0293 0.1298 0.1407 -0.0527 0.0340  -0.0649 244 TRP B CB  
4278 C  CG  . TRP B 244 ? 0.0281 0.1310 0.1387 -0.0506 0.0370  -0.0646 244 TRP B CG  
4279 C  CD1 . TRP B 244 ? 0.0332 0.1275 0.1172 -0.0538 0.0323  -0.0336 244 TRP B CD1 
4280 C  CD2 . TRP B 244 ? 0.0395 0.1220 0.1333 -0.0615 0.0359  -0.0561 244 TRP B CD2 
4281 N  NE1 . TRP B 244 ? 0.0247 0.1166 0.1344 -0.0417 0.0302  -0.0343 244 TRP B NE1 
4282 C  CE2 . TRP B 244 ? 0.0231 0.1132 0.1488 -0.0415 0.0237  -0.0383 244 TRP B CE2 
4283 C  CE3 . TRP B 244 ? 0.0263 0.1164 0.1363 -0.0445 0.0288  -0.0341 244 TRP B CE3 
4284 C  CZ2 . TRP B 244 ? 0.0375 0.1272 0.1470 -0.0577 0.0043  -0.0452 244 TRP B CZ2 
4285 C  CZ3 . TRP B 244 ? 0.0245 0.1172 0.1606 -0.0402 0.0048  -0.0506 244 TRP B CZ3 
4286 C  CH2 . TRP B 244 ? 0.0581 0.1079 0.1514 -0.0275 0.0044  -0.0352 244 TRP B CH2 
4287 N  N   . ARG B 245 ? 0.0203 0.1303 0.1186 -0.0415 0.0210  -0.0676 245 ARG B N   
4288 C  CA  . ARG B 245 ? 0.0205 0.1149 0.1377 -0.0375 0.0172  -0.0770 245 ARG B CA  
4289 C  C   . ARG B 245 ? 0.0145 0.1214 0.1203 -0.0304 0.0129  -0.0620 245 ARG B C   
4290 O  O   . ARG B 245 ? 0.0183 0.1494 0.1516 -0.0405 0.0145  -0.0772 245 ARG B O   
4291 C  CB  . ARG B 245 ? 0.0269 0.1340 0.1714 -0.0431 0.0064  -0.0912 245 ARG B CB  
4292 C  CG  . ARG B 245 ? 0.0229 0.1766 0.2217 -0.0487 0.0039  -0.0876 245 ARG B CG  
4293 C  CD  . ARG B 245 ? 0.0292 0.2042 0.2238 -0.0657 0.0352  -0.1397 245 ARG B CD  
4294 N  NE  . ARG B 245 ? 0.0229 0.1712 0.2277 -0.0510 0.0174  -0.0929 245 ARG B NE  
4295 C  CZ  . ARG B 245 ? 0.0174 0.1661 0.1656 -0.0391 0.0070  -0.0818 245 ARG B CZ  
4296 N  NH1 . ARG B 245 ? 0.0363 0.1320 0.1495 -0.0594 0.0177  -0.0677 245 ARG B NH1 
4297 N  NH2 . ARG B 245 ? 0.0454 0.1937 0.2198 -0.0813 0.0120  -0.0864 245 ARG B NH2 
4298 N  N   . PRO B 246 ? 0.0172 0.1075 0.1481 -0.0291 0.0306  -0.0462 246 PRO B N   
4299 C  CA  . PRO B 246 ? 0.0272 0.1172 0.1426 -0.0344 -0.0075 -0.0583 246 PRO B CA  
4300 C  C   . PRO B 246 ? 0.0158 0.1067 0.1424 -0.0209 -0.0013 -0.0451 246 PRO B C   
4301 O  O   . PRO B 246 ? 0.0136 0.1338 0.1710 -0.0252 -0.0016 -0.0754 246 PRO B O   
4302 C  CB  . PRO B 246 ? 0.0693 0.1420 0.1868 0.0138  0.0122  -0.0607 246 PRO B CB  
4303 C  CG  . PRO B 246 ? 0.0961 0.2544 0.2653 0.0110  0.0358  0.0397  246 PRO B CG  
4304 C  CD  . PRO B 246 ? 0.0126 0.1650 0.1860 -0.0091 0.0334  -0.0329 246 PRO B CD  
4305 N  N   . ALA B 247 ? 0.0189 0.1553 0.1499 -0.0432 0.0171  -0.0619 247 ALA B N   
4306 C  CA  . ALA B 247 ? 0.0318 0.1184 0.1470 -0.0433 0.0085  -0.0561 247 ALA B CA  
4307 C  C   . ALA B 247 ? 0.0160 0.1292 0.1398 -0.0099 0.0037  -0.0528 247 ALA B C   
4308 O  O   . ALA B 247 ? 0.0240 0.1389 0.1764 -0.0022 -0.0089 -0.0690 247 ALA B O   
4309 C  CB  . ALA B 247 ? 0.0529 0.1449 0.1816 -0.0444 0.0449  -0.0532 247 ALA B CB  
4310 N  N   . GLN B 248 ? 0.0212 0.1060 0.1623 -0.0364 0.0050  -0.0525 248 GLN B N   
4311 C  CA  . GLN B 248 ? 0.0159 0.1543 0.1617 -0.0324 -0.0103 -0.0388 248 GLN B CA  
4312 C  C   . GLN B 248 ? 0.0140 0.1342 0.1724 -0.0063 -0.0276 -0.0671 248 GLN B C   
4313 O  O   . GLN B 248 ? 0.0290 0.1649 0.1728 -0.0092 -0.0069 -0.0348 248 GLN B O   
4314 C  CB  . GLN B 248 ? 0.0279 0.1463 0.1676 -0.0386 -0.0144 -0.0623 248 GLN B CB  
4315 C  CG  . GLN B 248 ? 0.0324 0.1483 0.1580 -0.0324 0.0080  -0.0590 248 GLN B CG  
4316 C  CD  . GLN B 248 ? 0.0133 0.1989 0.1749 -0.0329 -0.0075 -0.0443 248 GLN B CD  
4317 O  OE1 . GLN B 248 ? 0.0192 0.2249 0.2137 -0.0410 -0.0137 -0.0770 248 GLN B OE1 
4318 N  NE2 . GLN B 248 ? 0.0278 0.1497 0.2087 -0.0486 -0.0136 -0.0487 248 GLN B NE2 
4319 N  N   . PRO B 249 ? 0.0151 0.1873 0.1747 -0.0203 -0.0253 -0.0543 249 PRO B N   
4320 C  CA  . PRO B 249 ? 0.0620 0.2020 0.1560 0.0167  -0.0234 -0.0401 249 PRO B CA  
4321 C  C   . PRO B 249 ? 0.0213 0.1495 0.1693 -0.0275 -0.0264 -0.0414 249 PRO B C   
4322 O  O   . PRO B 249 ? 0.0433 0.1599 0.1502 -0.0168 -0.0094 -0.0391 249 PRO B O   
4323 C  CB  . PRO B 249 ? 0.0947 0.2362 0.2147 0.0425  -0.0717 -0.0892 249 PRO B CB  
4324 C  CG  . PRO B 249 ? 0.1095 0.2940 0.1903 -0.0150 -0.0519 -0.0592 249 PRO B CG  
4325 C  CD  . PRO B 249 ? 0.0315 0.3041 0.2068 -0.0338 -0.0546 -0.0697 249 PRO B CD  
4326 N  N   . LEU B 250 ? 0.0578 0.1845 0.1579 0.0081  0.0072  -0.0409 250 LEU B N   
4327 C  CA  . LEU B 250 ? 0.0615 0.1298 0.1769 -0.0193 -0.0051 -0.0506 250 LEU B CA  
4328 C  C   . LEU B 250 ? 0.0987 0.1408 0.1461 -0.0147 -0.0185 -0.0425 250 LEU B C   
4329 O  O   . LEU B 250 ? 0.0764 0.1379 0.1748 -0.0153 -0.0386 -0.0682 250 LEU B O   
4330 C  CB  . LEU B 250 ? 0.0858 0.1690 0.2092 -0.0363 0.0179  -0.0483 250 LEU B CB  
4331 C  CG  . LEU B 250 ? 0.0685 0.2326 0.2099 -0.0414 0.0100  -0.0636 250 LEU B CG  
4332 C  CD1 . LEU B 250 ? 0.0383 0.2412 0.1983 -0.0306 -0.0004 -0.0864 250 LEU B CD1 
4333 C  CD2 . LEU B 250 ? 0.2566 0.2018 0.2418 -0.1047 0.0608  -0.1058 250 LEU B CD2 
4334 N  N   . LYS B 251 ? 0.0893 0.1857 0.1725 -0.0041 -0.0298 -0.0737 251 LYS B N   
4335 C  CA  . LYS B 251 ? 0.1324 0.2160 0.1398 -0.0029 -0.0249 -0.0750 251 LYS B CA  
4336 C  C   . LYS B 251 ? 0.0852 0.2129 0.1955 -0.0250 -0.0262 -0.0749 251 LYS B C   
4337 O  O   . LYS B 251 ? 0.1358 0.2712 0.2354 -0.0683 -0.0175 -0.0635 251 LYS B O   
4338 C  CB  . LYS B 251 ? 0.1826 0.2283 0.1771 -0.0203 -0.0177 -0.0778 251 LYS B CB  
4339 C  CG  . LYS B 251 ? 0.1055 0.3254 0.3353 -0.0751 0.0323  -0.1242 251 LYS B CG  
4340 C  CD  . LYS B 251 ? 0.1353 0.4337 0.4440 -0.1406 0.0475  -0.1258 251 LYS B CD  
4341 C  CE  . LYS B 251 ? 0.1489 0.4908 0.4577 -0.0522 0.0376  -0.0325 251 LYS B CE  
4342 N  NZ  . LYS B 251 ? 0.1242 0.4538 0.5768 -0.0561 0.0553  -0.0414 251 LYS B NZ  
4343 N  N   . ASN B 252 ? 0.1459 0.2156 0.1747 0.0121  -0.0662 -0.0917 252 ASN B N   
4344 C  CA  . ASN B 252 ? 0.0928 0.3541 0.2555 -0.0160 -0.0150 -0.1153 252 ASN B CA  
4345 C  C   . ASN B 252 ? 0.1980 0.3335 0.3247 0.0731  -0.0783 -0.1217 252 ASN B C   
4346 O  O   . ASN B 252 ? 0.2235 0.3197 0.3534 0.0568  -0.0442 -0.1142 252 ASN B O   
4347 C  CB  . ASN B 252 ? 0.1507 0.3693 0.2667 -0.0625 0.0317  -0.1112 252 ASN B CB  
4348 C  CG  . ASN B 252 ? 0.4265 0.3087 0.3367 -0.0790 0.0625  -0.2081 252 ASN B CG  
4349 O  OD1 . ASN B 252 ? 0.5008 0.6298 0.5719 -0.1969 0.1447  0.0029  252 ASN B OD1 
4350 N  ND2 . ASN B 252 ? 0.2451 0.3288 0.4487 -0.0497 0.0261  -0.1682 252 ASN B ND2 
4351 N  N   . ARG B 253 ? 0.0663 0.3327 0.2423 0.0214  -0.0077 -0.0688 253 ARG B N   
4352 C  CA  . ARG B 253 ? 0.0517 0.1696 0.1401 -0.0156 0.0115  -0.0704 253 ARG B CA  
4353 C  C   . ARG B 253 ? 0.0708 0.1697 0.1814 -0.0263 0.0103  -0.0628 253 ARG B C   
4354 O  O   . ARG B 253 ? 0.1688 0.2254 0.3010 0.0273  0.0726  0.0107  253 ARG B O   
4355 C  CB  . ARG B 253 ? 0.0726 0.1632 0.1341 -0.0168 0.0042  -0.0513 253 ARG B CB  
4356 C  CG  . ARG B 253 ? 0.0933 0.1356 0.1377 -0.0332 -0.0114 -0.0750 253 ARG B CG  
4357 C  CD  . ARG B 253 ? 0.0420 0.1567 0.1494 -0.0181 -0.0086 -0.0699 253 ARG B CD  
4358 N  NE  . ARG B 253 ? 0.0300 0.1313 0.1395 -0.0342 -0.0142 -0.0624 253 ARG B NE  
4359 C  CZ  . ARG B 253 ? 0.0183 0.1229 0.1227 -0.0313 0.0048  -0.0547 253 ARG B CZ  
4360 N  NH1 . ARG B 253 ? 0.0186 0.1515 0.1273 -0.0373 -0.0067 -0.0404 253 ARG B NH1 
4361 N  NH2 . ARG B 253 ? 0.0243 0.1461 0.1464 -0.0205 -0.0261 -0.0790 253 ARG B NH2 
4362 N  N   . GLN B 254 ? 0.0523 0.2109 0.1665 -0.0348 -0.0140 -0.1038 254 GLN B N   
4363 C  CA  . GLN B 254 ? 0.0432 0.2517 0.1931 -0.0226 -0.0053 -0.0702 254 GLN B CA  
4364 C  C   . GLN B 254 ? 0.0392 0.1549 0.1847 -0.0206 -0.0057 -0.0632 254 GLN B C   
4365 O  O   . GLN B 254 ? 0.1725 0.1606 0.2373 -0.0517 -0.0368 -0.0579 254 GLN B O   
4366 C  CB  . GLN B 254 ? 0.0732 0.5228 0.3265 -0.1312 0.1078  -0.1355 254 GLN B CB  
4367 C  CG  . GLN B 254 ? 0.2912 0.5964 0.2726 0.0002  0.0528  -0.2224 254 GLN B CG  
4368 C  CD  . GLN B 254 ? 0.5628 0.5653 0.3512 -0.2163 0.1637  -0.2683 254 GLN B CD  
4369 O  OE1 . GLN B 254 ? 0.9131 0.4882 0.7705 -0.0807 0.1368  -0.3594 254 GLN B OE1 
4370 N  NE2 . GLN B 254 ? 0.3476 0.4499 1.0139 -0.0666 0.2368  -0.0589 254 GLN B NE2 
4371 N  N   . ILE B 255 ? 0.0873 0.1521 0.1482 -0.0216 0.0188  -0.0658 255 ILE B N   
4372 C  CA  . ILE B 255 ? 0.0644 0.1557 0.1358 -0.0303 0.0299  -0.0456 255 ILE B CA  
4373 C  C   . ILE B 255 ? 0.0674 0.1703 0.1396 -0.0266 0.0337  -0.0298 255 ILE B C   
4374 O  O   . ILE B 255 ? 0.0990 0.2071 0.1813 -0.0057 0.0643  -0.0005 255 ILE B O   
4375 C  CB  . ILE B 255 ? 0.0516 0.1581 0.1615 -0.0307 0.0254  -0.0577 255 ILE B CB  
4376 C  CG1 . ILE B 255 ? 0.0340 0.1310 0.2121 -0.0099 0.0084  -0.0425 255 ILE B CG1 
4377 C  CG2 . ILE B 255 ? 0.0525 0.1915 0.1832 -0.0120 0.0140  -0.0745 255 ILE B CG2 
4378 C  CD1 . ILE B 255 ? 0.0931 0.1567 0.1729 -0.0616 0.0442  -0.0692 255 ILE B CD1 
4379 N  N   . LYS B 256 ? 0.0238 0.1362 0.1473 -0.0468 0.0124  -0.0564 256 LYS B N   
4380 C  CA  . LYS B 256 ? 0.0432 0.1321 0.1742 -0.0389 0.0436  -0.0472 256 LYS B CA  
4381 C  C   . LYS B 256 ? 0.0491 0.1582 0.1668 -0.0614 0.0416  -0.0376 256 LYS B C   
4382 O  O   . LYS B 256 ? 0.0947 0.1882 0.1435 -0.0778 0.0391  -0.0599 256 LYS B O   
4383 C  CB  . LYS B 256 ? 0.0856 0.1550 0.2079 -0.0408 0.0572  -0.0949 256 LYS B CB  
4384 C  CG  . LYS B 256 ? 0.0908 0.3030 0.2609 -0.0673 0.0553  -0.1157 256 LYS B CG  
4385 C  CD  . LYS B 256 ? 0.2042 0.2992 0.3686 -0.0432 -0.0136 -0.0741 256 LYS B CD  
4386 C  CE  . LYS B 256 ? 0.2018 0.5385 0.5279 -0.1229 0.0431  -0.2715 256 LYS B CE  
4387 N  NZ  . LYS B 256 ? 0.2253 0.5748 0.8052 -0.1571 0.2550  -0.1832 256 LYS B NZ  
4388 N  N   . ALA B 257 ? 0.0463 0.1553 0.1734 -0.0589 0.0584  -0.0534 257 ALA B N   
4389 C  CA  . ALA B 257 ? 0.0387 0.1585 0.2102 -0.0521 0.0418  -0.0398 257 ALA B CA  
4390 C  C   . ALA B 257 ? 0.0590 0.1694 0.1781 -0.0317 0.0403  -0.0530 257 ALA B C   
4391 O  O   . ALA B 257 ? 0.0863 0.1796 0.1958 -0.0514 0.0710  -0.0644 257 ALA B O   
4392 C  CB  . ALA B 257 ? 0.0678 0.1637 0.2387 -0.0602 0.0314  -0.0227 257 ALA B CB  
4393 N  N   . SER B 258 ? 0.0360 0.1634 0.1903 -0.0392 0.0339  -0.0489 258 SER B N   
4394 C  CA  . SER B 258 ? 0.0308 0.1743 0.2020 -0.0321 0.0412  -0.0431 258 SER B CA  
4395 C  C   . SER B 258 ? 0.0278 0.2099 0.2132 -0.0505 0.0411  -0.0526 258 SER B C   
4396 O  O   . SER B 258 ? 0.0393 0.4021 0.2827 -0.0129 0.0954  -0.0455 258 SER B O   
4397 C  CB  . SER B 258 ? 0.0534 0.1537 0.2065 -0.0453 0.0221  -0.0376 258 SER B CB  
4398 O  OG  . SER B 258 ? 0.0348 0.1964 0.2000 -0.0436 0.0446  -0.0608 258 SER B OG  
4399 N  N   . PHE B 259 ? 0.0451 0.2100 0.2742 -0.0399 0.0976  -0.0413 259 PHE B N   
4400 C  CA  . PHE B 259 ? 0.1265 0.2451 0.2843 -0.1167 0.0780  -0.0556 259 PHE B CA  
4401 C  C   . PHE B 259 ? 0.1676 0.3999 0.3274 -0.2015 0.1262  -0.0071 259 PHE B C   
4402 O  O   . PHE B 259 ? 0.1895 0.2763 0.3103 -0.1603 0.0778  0.0043  259 PHE B O   
4403 C  CB  . PHE B 259 ? 0.0875 0.2547 0.3000 -0.0983 0.0312  -0.0770 259 PHE B CB  
4404 C  CG  . PHE B 259 ? 0.0854 0.2105 0.2922 -0.0886 0.0161  -0.0637 259 PHE B CG  
4405 C  CD1 . PHE B 259 ? 0.0441 0.2244 0.2572 -0.0850 -0.0024 -0.0761 259 PHE B CD1 
4406 C  CD2 . PHE B 259 ? 0.1351 0.2454 0.3207 -0.0723 0.0462  -0.0351 259 PHE B CD2 
4407 C  CE1 . PHE B 259 ? 0.0873 0.2235 0.3412 -0.0597 0.0620  -0.0547 259 PHE B CE1 
4408 C  CE2 . PHE B 259 ? 0.1212 0.2491 0.4439 -0.0606 0.0359  -0.0104 259 PHE B CE2 
4409 C  CZ  . PHE B 259 ? 0.1544 0.2341 0.3462 -0.0858 0.0203  -0.0562 259 PHE B CZ  
4410 N  N   . LYS B 260 ? 0.3700 0.4376 0.4710 -0.3280 0.1992  -0.0326 260 LYS B N   
4411 C  CA  . LYS B 260 ? 0.6003 0.5420 0.5201 -0.0386 0.1128  0.1340  260 LYS B CA  
4412 C  C   . LYS B 260 ? 0.6175 0.5368 0.5462 -0.2120 0.0452  0.1234  260 LYS B C   
4413 O  O   . LYS B 260 ? 0.3463 0.9561 1.3944 -0.3836 -0.0158 0.0353  260 LYS B O   
4414 C  CB  . LYS B 260 ? 0.6659 0.4499 0.3599 -0.1518 0.1564  0.0761  260 LYS B CB  
4415 C  CG  . LYS B 260 ? 0.5210 0.3992 0.4502 -0.1571 0.1253  0.0552  260 LYS B CG  
4416 C  CD  . LYS B 260 ? 0.6013 0.6044 0.6455 0.0883  -0.0407 -0.0523 260 LYS B CD  
4417 C  CE  . LYS B 260 ? 0.2891 0.7198 0.5486 0.1150  -0.0249 0.0233  260 LYS B CE  
4418 N  NZ  . LYS B 260 ? 0.7805 1.0855 0.8098 -0.0366 -0.2351 -0.2247 260 LYS B NZ  
4419 O  OXT . LYS B 260 ? 0.5205 0.7747 0.8862 -0.3933 0.0521  0.0249  260 LYS B OXT 
4420 ZN ZN  . ZN  C .   ? 0.0165 0.0877 0.1149 -0.0274 0.0069  -0.0461 301 ZN  A ZN  
4421 CL CL  . 7VZ D .   ? 0.7409 0.3127 0.2795 -0.0513 0.1034  -0.1098 302 7VZ A CL  
4422 C  C10 . 7VZ D .   ? 0.2180 0.1438 0.2188 -0.0282 0.0697  -0.0898 302 7VZ A C10 
4423 C  C11 . 7VZ D .   ? 0.1119 0.1190 0.1547 -0.0074 0.0257  -0.0458 302 7VZ A C11 
4424 C  C14 . 7VZ D .   ? 0.0741 0.1408 0.1585 -0.0159 0.0156  -0.0409 302 7VZ A C14 
4425 O  O16 . 7VZ D .   ? 0.0832 0.1427 0.1172 -0.0166 0.0184  -0.0377 302 7VZ A O16 
4426 C  C17 . 7VZ D .   ? 0.0967 0.1586 0.1275 -0.0477 0.0146  -0.0232 302 7VZ A C17 
4427 O  O15 . 7VZ D .   ? 0.2419 0.1621 0.1635 -0.0346 0.0322  -0.0599 302 7VZ A O15 
4428 C  C9  . 7VZ D .   ? 0.2211 0.1552 0.2031 -0.0567 0.0460  -0.0833 302 7VZ A C9  
4429 C  C8  . 7VZ D .   ? 0.1914 0.1173 0.1734 -0.0283 -0.0314 -0.0424 302 7VZ A C8  
4430 C  C7  . 7VZ D .   ? 0.0517 0.1208 0.1447 -0.0220 -0.0275 -0.0428 302 7VZ A C7  
4431 S  S4  . 7VZ D .   ? 0.0403 0.1036 0.1387 -0.0245 -0.0111 -0.0444 302 7VZ A S4  
4432 O  O6  . 7VZ D .   ? 0.0484 0.1025 0.1509 -0.0370 -0.0152 -0.0376 302 7VZ A O6  
4433 N  N1  . 7VZ D .   ? 0.0104 0.1064 0.1415 0.0051  -0.0207 -0.0218 302 7VZ A N1  
4434 O  O5  . 7VZ D .   ? 0.0960 0.1124 0.1577 -0.0155 -0.0247 -0.0511 302 7VZ A O5  
4435 C  C12 . 7VZ D .   ? 0.0596 0.1217 0.1316 -0.0162 -0.0084 -0.0467 302 7VZ A C12 
4436 S  S21 . 7VZ D .   ? 0.1985 0.1412 0.2012 -0.0156 0.0270  -0.0536 302 7VZ A S21 
4437 C  C22 . 7VZ D .   ? 0.2080 0.1489 0.1735 0.0005  -0.0159 -0.0721 302 7VZ A C22 
4438 C  C23 . 7VZ D .   ? 0.1567 0.2264 0.1998 -0.0119 0.0372  -0.0660 302 7VZ A C23 
4439 C  C24 . 7VZ D .   ? 0.1663 0.1869 0.2839 -0.0934 -0.0147 -0.0730 302 7VZ A C24 
4440 C  C25 . 7VZ D .   ? 0.2740 0.1840 0.2755 0.0004  -0.0672 -0.0438 302 7VZ A C25 
4441 C  C26 . 7VZ D .   ? 0.1741 0.1701 0.2634 0.0127  -0.0205 -0.0379 302 7VZ A C26 
4442 C  C27 . 7VZ D .   ? 0.2632 0.1603 0.2363 -0.0036 -0.0111 -0.0414 302 7VZ A C27 
4443 C  C   . ACT E .   ? 0.5230 0.3714 0.3113 -0.0025 -0.0600 -0.1526 303 ACT A C   
4444 O  O   . ACT E .   ? 0.2364 0.3162 0.2215 -0.0903 -0.0060 0.0047  303 ACT A O   
4445 O  OXT . ACT E .   ? 0.6249 0.8662 0.5938 -0.0497 -0.1886 0.1292  303 ACT A OXT 
4446 C  CH3 . ACT E .   ? 0.1397 0.1848 0.2120 -0.0906 -0.0183 -0.0089 303 ACT A CH3 
4447 S  S   . DMS F .   ? 0.1057 0.2470 0.2848 -0.0238 0.0324  -0.0145 304 DMS A S   
4448 O  O   . DMS F .   ? 0.2563 0.2658 0.3429 -0.0685 0.0999  0.0050  304 DMS A O   
4449 C  C1  . DMS F .   ? 0.0552 0.2920 0.4117 0.0020  0.0442  -0.0012 304 DMS A C1  
4450 C  C2  . DMS F .   ? 0.1664 0.2094 0.2470 -0.0704 0.0461  -0.0402 304 DMS A C2  
4451 ZN ZN  . ZN  G .   ? 0.0320 0.1053 0.1212 -0.0474 0.0081  -0.0504 301 ZN  B ZN  
4452 CL CL  . 7VZ H .   ? 1.0494 0.3190 0.2700 -0.0326 0.1350  -0.0502 302 7VZ B CL  
4453 C  C10 . 7VZ H .   ? 0.3195 0.1359 0.1807 -0.0431 0.0070  -0.0617 302 7VZ B C10 
4454 C  C11 . 7VZ H .   ? 0.1389 0.1204 0.1732 -0.0768 0.0179  -0.0501 302 7VZ B C11 
4455 C  C14 . 7VZ H .   ? 0.0802 0.1419 0.1518 -0.0527 0.0248  -0.0369 302 7VZ B C14 
4456 O  O16 . 7VZ H .   ? 0.0888 0.1468 0.1238 -0.0584 0.0208  -0.0372 302 7VZ B O16 
4457 C  C17 . 7VZ H .   ? 0.1199 0.1563 0.1474 -0.0533 0.0087  -0.0694 302 7VZ B C17 
4458 O  O15 . 7VZ H .   ? 0.2716 0.1712 0.1643 -0.0467 0.0306  -0.0203 302 7VZ B O15 
4459 C  C9  . 7VZ H .   ? 0.3075 0.1318 0.1866 -0.0314 0.0103  -0.0545 302 7VZ B C9  
4460 C  C8  . 7VZ H .   ? 0.2195 0.1489 0.1596 -0.0497 -0.0249 -0.0636 302 7VZ B C8  
4461 C  C7  . 7VZ H .   ? 0.0872 0.1170 0.1548 -0.0655 -0.0079 -0.0549 302 7VZ B C7  
4462 S  S4  . 7VZ H .   ? 0.0533 0.1230 0.1469 -0.0633 -0.0125 -0.0486 302 7VZ B S4  
4463 O  O6  . 7VZ H .   ? 0.0982 0.1213 0.1676 -0.0778 -0.0379 -0.0510 302 7VZ B O6  
4464 N  N1  . 7VZ H .   ? 0.0302 0.1158 0.1536 -0.0507 0.0115  -0.0384 302 7VZ B N1  
4465 O  O5  . 7VZ H .   ? 0.0538 0.1311 0.1388 -0.0379 -0.0065 -0.0450 302 7VZ B O5  
4466 C  C12 . 7VZ H .   ? 0.0511 0.1364 0.1399 -0.0633 -0.0079 -0.0580 302 7VZ B C12 
4467 S  S21 . 7VZ H .   ? 0.2101 0.1353 0.2010 -0.0644 0.0236  -0.0482 302 7VZ B S21 
4468 C  C22 . 7VZ H .   ? 0.1344 0.1606 0.2101 -0.1174 -0.0125 -0.0412 302 7VZ B C22 
4469 C  C23 . 7VZ H .   ? 0.0869 0.2488 0.2412 -0.0882 0.0275  -0.0352 302 7VZ B C23 
4470 C  C24 . 7VZ H .   ? 0.2942 0.2037 0.2318 -0.0873 -0.0063 -0.0789 302 7VZ B C24 
4471 C  C25 . 7VZ H .   ? 0.3007 0.1479 0.3164 -0.1024 -0.0891 -0.0847 302 7VZ B C25 
4472 C  C26 . 7VZ H .   ? 0.2725 0.1370 0.2547 -0.1017 -0.0839 -0.0641 302 7VZ B C26 
4473 C  C27 . 7VZ H .   ? 0.2744 0.1221 0.2685 -0.0809 -0.0547 -0.0536 302 7VZ B C27 
4474 S  S   . DMS I .   ? 0.0919 0.2389 0.2718 -0.0807 0.0260  -0.0759 303 DMS B S   
4475 O  O   . DMS I .   ? 0.2965 0.2575 0.3445 0.0214  0.1029  -0.0956 303 DMS B O   
4476 C  C1  . DMS I .   ? 0.1026 0.4021 0.6302 -0.0622 0.2057  -0.0539 303 DMS B C1  
4477 C  C2  . DMS I .   ? 0.1524 0.2318 0.2198 -0.0154 0.0255  -0.0751 303 DMS B C2  
4478 O  O   . HOH J .   ? 0.9450 0.5893 0.2549 0.3180  0.0562  0.0407  401 HOH A O   
4479 O  O   . HOH J .   ? 1.3660 3.2888 1.9304 -1.8570 -1.5056 1.6187  402 HOH A O   
4480 O  O   . HOH J .   ? 0.3734 0.3906 0.5167 -0.2191 -0.0326 -0.0600 403 HOH A O   
4481 O  O   . HOH J .   ? 0.3073 0.7702 0.2397 -0.2931 0.0702  -0.1181 404 HOH A O   
4482 O  O   . HOH J .   ? 0.2388 0.3129 0.7146 -0.0557 -0.0375 -0.0956 405 HOH A O   
4483 O  O   . HOH J .   ? 0.2794 0.4698 0.4843 -0.0002 0.1690  -0.0253 406 HOH A O   
4484 O  O   . HOH J .   ? 0.3623 0.2232 0.2429 -0.1148 0.0406  -0.1196 407 HOH A O   
4485 O  O   . HOH J .   ? 0.6411 0.2319 0.4787 -0.1384 -0.1109 -0.1004 408 HOH A O   
4486 O  O   . HOH J .   ? 0.3330 0.3881 0.3986 -0.0330 -0.0147 -0.0122 409 HOH A O   
4487 O  O   . HOH J .   ? 0.5134 0.2308 0.2251 0.0057  -0.0264 -0.0154 410 HOH A O   
4488 O  O   . HOH J .   ? 0.1958 0.4303 0.4830 -0.0463 -0.0727 -0.1121 411 HOH A O   
4489 O  O   . HOH J .   ? 0.2947 0.3328 0.4125 0.0878  0.1166  0.0629  412 HOH A O   
4490 O  O   . HOH J .   ? 0.1819 0.6274 0.3607 -0.0902 -0.0478 -0.0359 413 HOH A O   
4491 O  O   . HOH J .   ? 0.1252 0.3242 0.3996 -0.0969 0.0397  0.0065  414 HOH A O   
4492 O  O   . HOH J .   ? 0.4489 0.7360 0.3588 0.3999  0.1382  0.0625  415 HOH A O   
4493 O  O   . HOH J .   ? 0.4928 0.7124 0.1961 -0.0129 -0.0111 -0.0841 416 HOH A O   
4494 O  O   . HOH J .   ? 0.2883 0.4022 0.3620 -0.0703 0.0387  0.0568  417 HOH A O   
4495 O  O   . HOH J .   ? 0.1049 0.4640 0.4834 -0.0908 0.0189  -0.1662 418 HOH A O   
4496 O  O   . HOH J .   ? 0.1676 0.2723 0.4253 0.0089  0.0937  0.0834  419 HOH A O   
4497 O  O   . HOH J .   ? 0.6065 0.2246 0.2588 -0.0373 0.0678  0.0067  420 HOH A O   
4498 O  O   . HOH J .   ? 0.2020 0.4237 0.5560 0.0666  0.1779  0.1269  421 HOH A O   
4499 O  O   . HOH J .   ? 0.1496 0.3581 0.5693 -0.0522 -0.0640 0.1405  422 HOH A O   
4500 O  O   . HOH J .   ? 0.1966 0.5145 0.4989 -0.1548 -0.0212 0.0049  423 HOH A O   
4501 O  O   . HOH J .   ? 0.2210 0.2947 0.6195 0.0674  0.0381  0.0238  424 HOH A O   
4502 O  O   . HOH J .   ? 0.2992 0.6121 0.4100 0.0780  0.0234  -0.0368 425 HOH A O   
4503 O  O   . HOH J .   ? 0.1919 0.4313 0.3785 -0.1672 0.0819  -0.0083 426 HOH A O   
4504 O  O   . HOH J .   ? 0.7353 0.3125 0.2439 0.0616  0.0528  -0.0063 427 HOH A O   
4505 O  O   . HOH J .   ? 0.4342 0.3732 0.7127 0.0116  -0.1614 -0.1349 428 HOH A O   
4506 O  O   . HOH J .   ? 0.2342 0.4740 0.5547 -0.0620 0.0009  0.0805  429 HOH A O   
4507 O  O   . HOH J .   ? 0.6887 0.3075 0.3805 0.0269  -0.0013 -0.1095 430 HOH A O   
4508 O  O   . HOH J .   ? 0.2390 0.6036 0.4557 0.0145  -0.0284 0.1948  431 HOH A O   
4509 O  O   . HOH J .   ? 0.1851 0.6508 0.9212 -0.0015 0.0362  0.0314  432 HOH A O   
4510 O  O   . HOH J .   ? 0.2915 0.2196 0.2558 0.0571  -0.0668 -0.0589 433 HOH A O   
4511 O  O   . HOH J .   ? 0.3833 0.3527 0.5899 0.0088  -0.0722 -0.1045 434 HOH A O   
4512 O  O   . HOH J .   ? 0.2022 0.2892 0.5863 -0.0759 0.0323  -0.0893 435 HOH A O   
4513 O  O   . HOH J .   ? 0.0361 0.6197 0.4780 -0.1219 0.0147  0.1690  436 HOH A O   
4514 O  O   . HOH J .   ? 0.4370 0.6495 0.6824 -0.2172 0.1637  -0.3474 437 HOH A O   
4515 O  O   . HOH J .   ? 0.1370 0.2313 0.3064 -0.1054 -0.0801 -0.0234 438 HOH A O   
4516 O  O   . HOH J .   ? 0.0192 0.1373 0.1860 -0.0372 -0.0089 -0.0387 439 HOH A O   
4517 O  O   . HOH J .   ? 0.2833 0.1960 0.2179 -0.0023 0.0088  -0.0938 440 HOH A O   
4518 O  O   . HOH J .   ? 0.1832 0.3762 0.3006 0.0260  0.0844  0.0165  441 HOH A O   
4519 O  O   . HOH J .   ? 0.2134 0.6188 0.4134 0.1188  -0.0175 -0.2806 442 HOH A O   
4520 O  O   . HOH J .   ? 0.4226 0.4566 0.2811 -0.0507 -0.0011 -0.1419 443 HOH A O   
4521 O  O   . HOH J .   ? 0.1409 0.2634 0.2931 -0.0474 -0.0741 0.0390  444 HOH A O   
4522 O  O   . HOH J .   ? 0.2471 0.6889 0.3473 0.0854  0.0619  -0.0773 445 HOH A O   
4523 O  O   . HOH J .   ? 0.7039 0.1425 0.3823 0.0150  -0.1140 -0.1808 446 HOH A O   
4524 O  O   . HOH J .   ? 0.2940 0.2446 0.3146 -0.1658 -0.0828 -0.0380 447 HOH A O   
4525 O  O   . HOH J .   ? 0.2185 0.3173 0.4555 0.0109  -0.0181 -0.1012 448 HOH A O   
4526 O  O   . HOH J .   ? 0.1664 0.1907 0.2837 -0.0308 -0.0514 -0.0444 449 HOH A O   
4527 O  O   . HOH J .   ? 0.4352 0.5119 0.6208 -0.2126 0.0254  -0.1991 450 HOH A O   
4528 O  O   . HOH J .   ? 0.3046 0.4874 0.6443 -0.0661 -0.0649 -0.1177 451 HOH A O   
4529 O  O   . HOH J .   ? 0.0186 0.1190 0.1668 -0.0316 0.0331  -0.0388 452 HOH A O   
4530 O  O   . HOH J .   ? 0.1186 0.2071 0.3701 -0.0277 0.0242  -0.0100 453 HOH A O   
4531 O  O   . HOH J .   ? 0.7372 0.3207 0.1673 0.0737  0.0252  -0.0343 454 HOH A O   
4532 O  O   . HOH J .   ? 0.2045 0.2772 0.2311 -0.0587 -0.0198 -0.0540 455 HOH A O   
4533 O  O   . HOH J .   ? 0.3309 0.8505 0.4232 0.0528  0.0362  -0.2998 456 HOH A O   
4534 O  O   . HOH J .   ? 0.1825 0.2280 0.4337 -0.0858 -0.0904 0.0081  457 HOH A O   
4535 O  O   . HOH J .   ? 0.2133 0.3084 0.3507 -0.1117 -0.1005 -0.0149 458 HOH A O   
4536 O  O   . HOH J .   ? 0.2680 0.6580 0.4704 -0.0803 0.1182  0.0307  459 HOH A O   
4537 O  O   . HOH J .   ? 0.6178 0.2592 0.5672 -0.0582 -0.1181 -0.1231 460 HOH A O   
4538 O  O   . HOH J .   ? 0.3162 0.3202 0.3066 0.0013  -0.0916 -0.1058 461 HOH A O   
4539 O  O   . HOH J .   ? 0.1183 0.2799 0.3378 -0.0427 0.1253  -0.0128 462 HOH A O   
4540 O  O   . HOH J .   ? 0.1391 0.5719 0.4901 -0.0002 0.0039  0.2055  463 HOH A O   
4541 O  O   . HOH J .   ? 0.0404 0.1755 0.1739 -0.0607 -0.0221 -0.0567 464 HOH A O   
4542 O  O   . HOH J .   ? 0.0615 0.1855 0.2404 -0.0398 -0.0063 -0.0810 465 HOH A O   
4543 O  O   . HOH J .   ? 0.4510 0.2308 0.3450 -0.0479 -0.1614 -0.0087 466 HOH A O   
4544 O  O   . HOH J .   ? 0.1682 0.3030 0.2340 0.0203  0.0525  -0.0544 467 HOH A O   
4545 O  O   . HOH J .   ? 0.0190 0.1287 0.1665 -0.0381 0.0269  -0.0543 468 HOH A O   
4546 O  O   . HOH J .   ? 0.1231 0.1911 0.3242 -0.0810 -0.1143 0.0146  469 HOH A O   
4547 O  O   . HOH J .   ? 0.3499 0.4759 0.4400 0.0174  0.1606  -0.0364 470 HOH A O   
4548 O  O   . HOH J .   ? 0.0754 0.2530 0.2456 -0.0712 0.0352  -0.0086 471 HOH A O   
4549 O  O   . HOH J .   ? 0.0262 0.1195 0.1369 -0.0447 0.0071  -0.0395 472 HOH A O   
4550 O  O   . HOH J .   ? 0.1744 0.2435 0.4887 -0.0759 -0.0569 0.0124  473 HOH A O   
4551 O  O   . HOH J .   ? 0.0445 0.1285 0.1460 -0.0262 0.0141  -0.0294 474 HOH A O   
4552 O  O   . HOH J .   ? 0.1164 0.2556 0.3009 -0.0888 -0.0120 -0.0242 475 HOH A O   
4553 O  O   . HOH J .   ? 0.2088 0.2058 0.7179 -0.0651 0.0230  0.0181  476 HOH A O   
4554 O  O   . HOH J .   ? 0.3698 0.3486 0.2851 0.0923  -0.1028 -0.0734 477 HOH A O   
4555 O  O   . HOH J .   ? 0.2843 0.3327 0.6414 0.0436  -0.0146 -0.0118 478 HOH A O   
4556 O  O   . HOH J .   ? 0.1776 0.3472 0.2874 0.0089  0.0595  0.0413  479 HOH A O   
4557 O  O   . HOH J .   ? 0.2541 0.1571 0.3236 -0.0873 -0.1542 -0.0221 480 HOH A O   
4558 O  O   . HOH J .   ? 0.2166 0.4089 0.5954 0.0992  -0.1213 -0.0211 481 HOH A O   
4559 O  O   . HOH J .   ? 0.0458 0.2297 0.3676 -0.0718 -0.0008 0.0168  482 HOH A O   
4560 O  O   . HOH J .   ? 0.0708 0.3910 0.6269 -0.0499 0.0145  -0.0994 483 HOH A O   
4561 O  O   . HOH J .   ? 0.1109 0.4688 0.4292 0.0025  -0.1243 -0.1199 484 HOH A O   
4562 O  O   . HOH J .   ? 0.2395 0.7416 0.3580 -0.0467 0.0671  -0.1533 485 HOH A O   
4563 O  O   . HOH J .   ? 0.0754 0.1452 0.1926 -0.0883 0.0073  -0.0662 486 HOH A O   
4564 O  O   . HOH J .   ? 0.4823 0.4871 0.7530 0.1937  0.2197  0.0829  487 HOH A O   
4565 O  O   . HOH J .   ? 0.8165 0.2357 0.2803 0.0334  0.0176  -0.0773 488 HOH A O   
4566 O  O   . HOH J .   ? 0.2497 0.3759 0.2106 0.0938  0.0534  -0.0071 489 HOH A O   
4567 O  O   . HOH J .   ? 0.4351 0.3300 0.3646 0.0155  0.2375  0.0476  490 HOH A O   
4568 O  O   . HOH J .   ? 0.2115 0.3879 0.2375 -0.0131 -0.0714 -0.1377 491 HOH A O   
4569 O  O   . HOH J .   ? 0.3407 0.2002 0.2985 0.0012  0.0283  -0.0530 492 HOH A O   
4570 O  O   . HOH J .   ? 0.3872 0.5121 0.6128 0.1770  0.2252  0.1357  493 HOH A O   
4571 O  O   . HOH J .   ? 0.0897 0.1603 0.3491 -0.0040 0.0087  -0.0403 494 HOH A O   
4572 O  O   . HOH J .   ? 0.2184 0.4092 0.6342 -0.0679 -0.1421 0.0431  495 HOH A O   
4573 O  O   . HOH J .   ? 0.3013 0.3013 0.2782 0.0859  0.1092  -0.0308 496 HOH A O   
4574 O  O   . HOH J .   ? 0.3201 0.4407 0.6758 -0.1076 0.0618  0.0631  497 HOH A O   
4575 O  O   . HOH J .   ? 0.0719 0.2056 0.4266 -0.0407 0.0052  0.0171  498 HOH A O   
4576 O  O   . HOH J .   ? 0.4313 0.3411 0.4411 0.1264  0.1360  -0.0618 499 HOH A O   
4577 O  O   . HOH J .   ? 0.0344 0.1391 0.1500 -0.0611 0.0212  -0.0417 500 HOH A O   
4578 O  O   . HOH J .   ? 0.0727 0.1657 0.2121 -0.0461 0.0113  -0.0519 501 HOH A O   
4579 O  O   . HOH J .   ? 0.1688 0.3375 0.5523 -0.0640 0.0100  -0.1625 502 HOH A O   
4580 O  O   . HOH J .   ? 0.0168 0.1779 0.4309 -0.0408 -0.0076 -0.0435 503 HOH A O   
4581 O  O   . HOH J .   ? 0.1277 0.2925 0.3730 -0.0384 0.1219  -0.0656 504 HOH A O   
4582 O  O   . HOH J .   ? 0.3527 0.2919 0.6105 -0.0353 -0.0147 -0.0364 505 HOH A O   
4583 O  O   . HOH J .   ? 0.8133 0.4132 0.3576 -0.1562 0.2405  -0.0745 506 HOH A O   
4584 O  O   . HOH J .   ? 0.2759 0.3074 0.3964 0.0396  -0.1367 -0.0986 507 HOH A O   
4585 O  O   . HOH J .   ? 0.3620 0.2572 0.3125 0.0921  -0.0751 -0.0697 508 HOH A O   
4586 O  O   . HOH J .   ? 0.3895 0.3177 0.6725 0.0687  -0.1935 0.0561  509 HOH A O   
4587 O  O   . HOH J .   ? 0.0940 0.2938 0.3843 -0.0012 0.0425  -0.0150 510 HOH A O   
4588 O  O   . HOH J .   ? 0.1076 0.2050 0.5899 0.0043  -0.0189 -0.0408 511 HOH A O   
4589 O  O   . HOH J .   ? 0.1356 0.2357 0.2024 -0.0678 0.0272  -0.0370 512 HOH A O   
4590 O  O   . HOH J .   ? 0.5719 0.6790 0.4934 -0.1167 -0.0095 0.1246  513 HOH A O   
4591 O  O   . HOH J .   ? 0.1414 0.3260 0.5304 0.0041  0.0726  -0.1562 514 HOH A O   
4592 O  O   . HOH J .   ? 0.2740 0.4540 0.7865 0.0900  0.1045  -0.0285 515 HOH A O   
4593 O  O   . HOH J .   ? 0.1300 0.3660 0.3409 -0.0934 -0.0219 -0.1503 516 HOH A O   
4594 O  O   . HOH J .   ? 0.1694 0.6079 0.9715 -0.0292 0.2822  0.1372  517 HOH A O   
4595 O  O   . HOH J .   ? 0.0987 0.4029 0.2053 -0.0705 0.0023  -0.0211 518 HOH A O   
4596 O  O   . HOH J .   ? 0.1566 0.1418 0.2168 -0.0238 -0.0115 -0.0411 519 HOH A O   
4597 O  O   . HOH J .   ? 0.0662 0.4218 0.3579 -0.0620 0.0494  -0.0398 520 HOH A O   
4598 O  O   . HOH J .   ? 0.2544 0.1921 0.3677 -0.0298 0.1100  -0.1384 521 HOH A O   
4599 O  O   . HOH J .   ? 0.1697 0.3260 0.4844 -0.0660 -0.0523 0.0026  522 HOH A O   
4600 O  O   . HOH J .   ? 0.3186 0.3452 0.2615 -0.1817 -0.0006 -0.0413 523 HOH A O   
4601 O  O   . HOH J .   ? 0.1127 0.2320 0.3310 -0.1004 -0.0122 -0.0388 524 HOH A O   
4602 O  O   . HOH J .   ? 0.6135 0.2836 0.2884 -0.1811 0.0882  -0.1329 525 HOH A O   
4603 O  O   . HOH J .   ? 0.0349 0.1568 0.1829 -0.0574 -0.0127 -0.0519 526 HOH A O   
4604 O  O   . HOH J .   ? 0.7144 0.2421 0.6907 0.0888  -0.4457 -0.0386 527 HOH A O   
4605 O  O   . HOH J .   ? 0.0309 0.2255 0.3288 -0.0734 0.0081  -0.0134 528 HOH A O   
4606 O  O   . HOH J .   ? 0.3986 0.5157 0.8236 -0.0543 -0.0890 -0.3895 529 HOH A O   
4607 O  O   . HOH J .   ? 0.3546 0.3035 0.2696 0.0529  0.0358  -0.1101 530 HOH A O   
4608 O  O   . HOH J .   ? 0.4436 0.4401 0.6664 0.0929  -0.1835 -0.3167 531 HOH A O   
4609 O  O   . HOH J .   ? 0.1192 0.5210 0.4538 -0.0075 0.0637  -0.1115 532 HOH A O   
4610 O  O   . HOH J .   ? 0.1297 0.4153 0.5259 -0.0366 -0.0181 -0.0963 533 HOH A O   
4611 O  O   . HOH J .   ? 0.2055 0.2391 0.2613 -0.1575 -0.0619 -0.0296 534 HOH A O   
4612 O  O   . HOH J .   ? 0.1719 0.4333 0.4184 0.0256  0.0227  -0.0873 535 HOH A O   
4613 O  O   . HOH J .   ? 0.2213 0.4599 0.3716 -0.1986 0.0736  -0.0501 536 HOH A O   
4614 O  O   . HOH J .   ? 0.4950 0.2776 0.2461 0.0693  0.0261  0.0229  537 HOH A O   
4615 O  O   . HOH J .   ? 0.0301 0.1749 0.2355 -0.0144 -0.0162 -0.0332 538 HOH A O   
4616 O  O   . HOH J .   ? 0.1890 0.1904 0.5844 -0.0008 -0.1285 -0.1172 539 HOH A O   
4617 O  O   . HOH J .   ? 0.2685 0.2160 0.4723 -0.1079 0.0040  -0.0672 540 HOH A O   
4618 O  O   . HOH J .   ? 0.0843 0.1969 0.2881 -0.0177 0.0589  -0.0109 541 HOH A O   
4619 O  O   . HOH J .   ? 0.4777 0.2944 0.7738 0.0075  -0.1732 0.0298  542 HOH A O   
4620 O  O   . HOH J .   ? 0.2861 0.1610 0.2930 -0.0231 -0.1450 -0.0883 543 HOH A O   
4621 O  O   . HOH J .   ? 0.4798 0.2782 0.6178 -0.0153 -0.2130 -0.0259 544 HOH A O   
4622 O  O   . HOH J .   ? 0.1760 0.1993 0.4513 -0.0531 0.0612  -0.1410 545 HOH A O   
4623 O  O   . HOH J .   ? 0.1750 0.2741 0.3705 -0.0855 0.0922  -0.0078 546 HOH A O   
4624 O  O   . HOH J .   ? 0.0457 0.2162 0.2394 -0.0772 0.0098  -0.0547 547 HOH A O   
4625 O  O   . HOH J .   ? 0.1566 0.2432 0.3572 -0.0983 0.0573  -0.0754 548 HOH A O   
4626 O  O   . HOH J .   ? 0.6667 0.4813 0.4875 -0.1371 -0.2054 0.1687  549 HOH A O   
4627 O  O   . HOH J .   ? 0.1439 0.4569 0.7379 0.0862  0.2285  0.1553  550 HOH A O   
4628 O  O   . HOH J .   ? 0.2165 0.1924 0.6434 -0.0484 0.0839  0.0584  551 HOH A O   
4629 O  O   . HOH J .   ? 0.2315 0.2482 0.2785 0.0102  -0.0425 -0.0524 552 HOH A O   
4630 O  O   . HOH J .   ? 0.2438 0.2867 0.3512 -0.0255 -0.0098 -0.0065 553 HOH A O   
4631 O  O   . HOH J .   ? 0.2089 0.2014 0.2773 0.0195  -0.0398 -0.1031 554 HOH A O   
4632 O  O   . HOH J .   ? 0.2868 0.3127 0.4546 -0.0980 -0.0602 0.0365  555 HOH A O   
4633 O  O   . HOH J .   ? 0.3289 0.2368 0.3533 -0.0696 0.1826  -0.0234 556 HOH A O   
4634 O  O   . HOH J .   ? 0.2259 0.1410 0.2785 -0.0378 -0.0629 0.0131  557 HOH A O   
4635 O  O   . HOH J .   ? 0.1555 0.1838 0.2337 -0.0904 -0.0343 -0.0089 558 HOH A O   
4636 O  O   . HOH J .   ? 0.1176 0.3485 0.3411 -0.0570 -0.0139 0.0367  559 HOH A O   
4637 O  O   . HOH J .   ? 0.7962 0.2545 0.3588 0.0890  -0.0508 -0.0601 560 HOH A O   
4638 O  O   . HOH J .   ? 0.5475 0.2384 0.3012 0.0860  -0.2046 -0.0546 561 HOH A O   
4639 O  O   . HOH J .   ? 0.1815 0.4167 0.3419 -0.1043 -0.0694 0.0283  562 HOH A O   
4640 O  O   . HOH J .   ? 0.0586 0.2945 0.3107 -0.0704 -0.0741 -0.0961 563 HOH A O   
4641 O  O   . HOH J .   ? 0.4169 0.5981 0.7478 0.0223  0.0231  -0.0908 564 HOH A O   
4642 O  O   . HOH J .   ? 0.2015 0.3847 0.3755 -0.1557 0.0666  -0.0587 565 HOH A O   
4643 O  O   . HOH J .   ? 0.1740 0.2445 0.2891 -0.0822 0.0121  -0.0716 566 HOH A O   
4644 O  O   . HOH J .   ? 0.2090 0.1961 0.2764 -0.0520 0.0582  -0.1316 567 HOH A O   
4645 O  O   . HOH J .   ? 0.4323 0.1729 0.2462 -0.0292 -0.1275 -0.0768 568 HOH A O   
4646 O  O   . HOH J .   ? 0.2010 0.4650 0.5962 -0.1395 0.1072  -0.1071 569 HOH A O   
4647 O  O   . HOH J .   ? 0.2469 0.3810 0.2417 -0.1676 -0.0812 -0.0710 570 HOH A O   
4648 O  O   . HOH J .   ? 0.2101 0.3155 0.3808 -0.0390 0.0388  -0.1944 571 HOH A O   
4649 O  O   . HOH J .   ? 0.4119 0.5427 0.5298 -0.1074 0.1042  -0.1264 572 HOH A O   
4650 O  O   . HOH J .   ? 0.5624 0.3929 0.3516 -0.2672 0.0559  -0.0776 573 HOH A O   
4651 O  O   . HOH J .   ? 0.2459 0.5061 0.3119 -0.1868 0.1069  -0.2103 574 HOH A O   
4652 O  O   . HOH J .   ? 0.5348 0.3039 0.3871 0.0547  0.0156  -0.0344 575 HOH A O   
4653 O  O   . HOH J .   ? 0.4343 0.4592 0.4392 -0.2396 0.0681  -0.1224 576 HOH A O   
4654 O  O   . HOH J .   ? 0.2393 0.4846 0.5163 -0.1813 -0.0145 0.0648  577 HOH A O   
4655 O  O   . HOH J .   ? 0.2092 0.5280 0.4870 0.1213  0.1140  0.0934  578 HOH A O   
4656 O  O   . HOH J .   ? 0.0366 0.1331 0.1716 -0.0594 0.0055  -0.0509 579 HOH A O   
4657 O  O   . HOH J .   ? 0.2237 0.2584 0.4364 -0.0381 0.0141  -0.0155 580 HOH A O   
4658 O  O   . HOH J .   ? 0.5967 0.3588 0.3444 -0.1005 -0.0833 0.0538  581 HOH A O   
4659 O  O   . HOH J .   ? 0.2992 0.1760 0.3721 -0.0767 -0.0017 -0.1399 582 HOH A O   
4660 O  O   . HOH J .   ? 0.6030 0.2056 0.3684 -0.1135 0.0732  -0.0536 583 HOH A O   
4661 O  O   . HOH J .   ? 0.3802 0.4582 0.4084 -0.0839 -0.0816 0.0138  584 HOH A O   
4662 O  O   . HOH J .   ? 0.2992 0.4062 0.4430 0.0496  0.0569  -0.0388 585 HOH A O   
4663 O  O   . HOH J .   ? 0.4236 0.2964 0.4784 -0.0251 0.2004  -0.1426 586 HOH A O   
4664 O  O   . HOH J .   ? 0.2791 0.3315 0.5516 -0.1727 0.0686  -0.1867 587 HOH A O   
4665 O  O   . HOH J .   ? 0.4953 0.3338 0.5941 -0.1173 0.1233  -0.1156 588 HOH A O   
4666 O  O   . HOH J .   ? 0.6023 0.2761 0.9729 -0.1249 -0.0136 0.0147  589 HOH A O   
4667 O  O   . HOH J .   ? 0.2388 0.2037 0.2375 -0.0925 -0.0165 -0.0778 590 HOH A O   
4668 O  O   . HOH J .   ? 0.7032 0.2067 0.4446 -0.0156 -0.3258 -0.0447 591 HOH A O   
4669 O  O   . HOH J .   ? 0.2842 0.2025 0.2824 -0.1057 0.0697  -0.1071 592 HOH A O   
4670 O  O   . HOH J .   ? 0.2606 0.4297 0.4551 -0.1946 0.0068  -0.0417 593 HOH A O   
4671 O  O   . HOH J .   ? 0.1690 0.2958 0.5319 -0.1013 0.0822  -0.1860 594 HOH A O   
4672 O  O   . HOH J .   ? 0.2845 0.4695 0.7101 0.0499  0.1459  -0.0188 595 HOH A O   
4673 O  O   . HOH J .   ? 0.2215 0.3053 0.4875 -0.0033 0.0719  0.0029  596 HOH A O   
4674 O  O   . HOH J .   ? 0.3235 0.3001 0.3355 -0.0597 -0.1248 -0.0477 597 HOH A O   
4675 O  O   . HOH J .   ? 0.6019 0.5205 0.4912 0.1544  0.2639  0.0593  598 HOH A O   
4676 O  O   . HOH J .   ? 0.6114 0.1409 0.3155 -0.0447 -0.2520 -0.0402 599 HOH A O   
4677 O  O   . HOH J .   ? 0.2919 0.3051 0.7957 -0.0105 0.0595  -0.1307 600 HOH A O   
4678 O  O   . HOH J .   ? 0.0511 0.2180 0.3808 -0.0522 -0.0022 -0.0168 601 HOH A O   
4679 O  O   . HOH J .   ? 0.1910 0.1807 0.2564 -0.1208 0.0302  -0.0304 602 HOH A O   
4680 O  O   . HOH J .   ? 1.0810 0.5037 1.0551 0.1324  -0.5583 -0.1307 603 HOH A O   
4681 O  O   . HOH J .   ? 0.2578 0.5504 0.4115 -0.1317 -0.0982 -0.0146 604 HOH A O   
4682 O  O   . HOH J .   ? 0.3837 0.5453 0.4127 0.1198  -0.0311 -0.1063 605 HOH A O   
4683 O  O   . HOH J .   ? 0.2931 0.3749 0.3194 -0.1680 -0.0250 0.0208  606 HOH A O   
4684 O  O   . HOH J .   ? 0.6597 0.4986 0.2239 -0.2870 -0.0835 -0.0264 607 HOH A O   
4685 O  O   . HOH J .   ? 0.1639 0.3538 0.3348 -0.1245 0.0570  -0.1791 608 HOH A O   
4686 O  O   . HOH J .   ? 0.3455 0.7360 0.2843 -0.1891 -0.0159 -0.1408 609 HOH A O   
4687 O  O   . HOH J .   ? 0.2946 0.3074 0.8540 -0.0637 0.1315  -0.0285 610 HOH A O   
4688 O  O   . HOH J .   ? 0.3078 0.4468 0.4256 -0.0994 -0.0651 0.0697  611 HOH A O   
4689 O  O   . HOH J .   ? 0.1967 0.4418 0.4914 0.0284  0.0807  -0.1342 612 HOH A O   
4690 O  O   . HOH J .   ? 0.5813 0.7534 0.6597 0.2436  0.0279  0.1060  613 HOH A O   
4691 O  O   . HOH J .   ? 0.8760 0.8126 0.3335 -0.4492 -0.0853 -0.0507 614 HOH A O   
4692 O  O   . HOH J .   ? 0.2279 1.0283 0.5737 0.1127  0.0195  -0.0921 615 HOH A O   
4693 O  O   . HOH J .   ? 0.3858 0.1608 0.3739 -0.0160 -0.1560 -0.0990 616 HOH A O   
4694 O  O   . HOH J .   ? 0.0759 0.1586 0.2617 -0.0496 -0.0041 -0.0433 617 HOH A O   
4695 O  O   . HOH J .   ? 0.3590 0.3561 0.4184 -0.1305 0.0108  -0.0957 618 HOH A O   
4696 O  O   . HOH J .   ? 0.5484 0.4763 0.2818 0.1430  -0.0995 -0.2585 619 HOH A O   
4697 O  O   . HOH J .   ? 0.2949 0.8643 0.3978 0.1209  -0.0119 -0.0419 620 HOH A O   
4698 O  O   . HOH J .   ? 0.4072 0.6255 0.6803 0.0389  -0.1583 -0.1241 621 HOH A O   
4699 O  O   . HOH J .   ? 0.3844 0.6282 0.4362 -0.1861 -0.0259 0.0308  622 HOH A O   
4700 O  O   . HOH J .   ? 0.4228 0.4491 0.5732 -0.2694 0.2190  -0.3326 623 HOH A O   
4701 O  O   . HOH J .   ? 0.2626 0.3326 0.5407 -0.0815 0.1421  -0.1012 624 HOH A O   
4702 O  O   . HOH J .   ? 0.1688 0.2975 0.4127 -0.0782 0.0301  -0.1275 625 HOH A O   
4703 O  O   . HOH J .   ? 0.3887 0.6406 0.8653 -0.0399 0.2644  0.1312  626 HOH A O   
4704 O  O   . HOH J .   ? 0.9111 0.3279 0.4867 0.1812  0.0138  -0.0889 627 HOH A O   
4705 O  O   . HOH J .   ? 0.2339 0.2938 0.2231 -0.0211 0.0070  -0.1083 628 HOH A O   
4706 O  O   . HOH J .   ? 0.5320 0.5934 0.3464 0.1494  0.1235  -0.1173 629 HOH A O   
4707 O  O   . HOH J .   ? 0.1462 0.3825 0.3823 -0.0314 0.0240  -0.0335 630 HOH A O   
4708 O  O   . HOH J .   ? 0.2199 0.7498 0.6016 0.1187  0.0436  0.1716  631 HOH A O   
4709 O  O   . HOH J .   ? 0.2814 0.4628 0.5209 -0.1678 0.0862  -0.2324 632 HOH A O   
4710 O  O   . HOH J .   ? 0.7372 0.3477 0.8631 -0.0144 0.2407  0.0731  633 HOH A O   
4711 O  O   . HOH J .   ? 0.3525 0.3579 0.3898 -0.1120 0.0741  -0.0253 634 HOH A O   
4712 O  O   . HOH J .   ? 0.3914 0.3670 0.7310 -0.1367 0.1747  -0.1145 635 HOH A O   
4713 O  O   . HOH J .   ? 0.6380 0.7217 0.8228 -0.2720 0.5109  -0.1903 636 HOH A O   
4714 O  O   . HOH J .   ? 0.1874 0.4402 0.4174 0.1084  0.0170  -0.0810 637 HOH A O   
4715 O  O   . HOH J .   ? 0.2513 0.2806 0.4415 -0.0912 -0.1777 0.0122  638 HOH A O   
4716 O  O   . HOH J .   ? 0.8239 0.3517 0.2997 -0.1830 0.0658  -0.0683 639 HOH A O   
4717 O  O   . HOH J .   ? 0.0727 0.7470 0.6398 -0.0600 0.0556  -0.0156 640 HOH A O   
4718 O  O   . HOH J .   ? 0.1576 0.4164 0.5147 -0.0401 0.0902  -0.1444 641 HOH A O   
4719 O  O   . HOH J .   ? 0.1314 0.3265 0.4665 -0.0841 -0.0273 -0.1186 642 HOH A O   
4720 O  O   . HOH J .   ? 0.4974 0.5969 0.3270 0.0095  -0.1080 -0.1551 643 HOH A O   
4721 O  O   . HOH J .   ? 0.7590 0.4332 0.3015 -0.2192 0.2139  -0.0876 644 HOH A O   
4722 O  O   . HOH J .   ? 0.4762 0.4898 0.3307 0.1383  0.0032  -0.1068 645 HOH A O   
4723 O  O   . HOH J .   ? 0.2989 0.3973 0.2961 -0.0449 -0.0670 -0.0688 646 HOH A O   
4724 O  O   . HOH J .   ? 0.4523 0.3784 0.5511 0.0748  -0.0859 -0.1081 647 HOH A O   
4725 O  O   . HOH J .   ? 0.4039 0.3213 0.4632 -0.1044 -0.1262 -0.0927 648 HOH A O   
4726 O  O   . HOH J .   ? 0.2175 0.2972 0.4367 -0.0416 0.0672  -0.0643 649 HOH A O   
4727 O  O   . HOH J .   ? 0.1649 0.3791 0.3689 -0.0686 -0.0122 -0.0939 650 HOH A O   
4728 O  O   . HOH J .   ? 0.2337 0.3759 0.7462 0.0120  -0.0644 -0.0513 651 HOH A O   
4729 O  O   . HOH J .   ? 0.1319 0.2559 0.4903 -0.0447 -0.0586 -0.1230 652 HOH A O   
4730 O  O   . HOH J .   ? 0.1152 0.4424 0.5741 -0.0682 -0.0709 0.0276  653 HOH A O   
4731 O  O   . HOH J .   ? 0.2364 0.4743 0.3957 -0.1034 0.0000  -0.0919 654 HOH A O   
4732 O  O   . HOH J .   ? 0.6071 0.5373 0.3499 -0.2827 0.1234  -0.2108 655 HOH A O   
4733 O  O   . HOH J .   ? 0.5234 0.3633 0.5960 0.1034  -0.2608 -0.1692 656 HOH A O   
4734 O  O   . HOH J .   ? 0.2103 0.2254 0.3097 -0.0555 0.0650  -0.1314 657 HOH A O   
4735 O  O   . HOH J .   ? 0.2123 0.4391 0.4112 -0.1697 0.0348  -0.0886 658 HOH A O   
4736 O  O   . HOH J .   ? 0.2633 0.6005 0.6807 -0.1597 0.0417  -0.1830 659 HOH A O   
4737 O  O   . HOH J .   ? 0.3017 0.2564 0.4757 -0.0763 -0.1285 -0.0921 660 HOH A O   
4738 O  O   . HOH J .   ? 0.1433 0.2134 0.2240 -0.0317 -0.0113 -0.0708 661 HOH A O   
4739 O  O   . HOH J .   ? 0.3202 0.3915 0.7806 -0.0361 -0.1539 0.0161  662 HOH A O   
4740 O  O   . HOH J .   ? 0.6541 0.6718 0.6061 -0.2065 0.1024  0.1328  663 HOH A O   
4741 O  O   . HOH J .   ? 0.6758 0.3334 0.4054 -0.1301 -0.0678 0.0575  664 HOH A O   
4742 O  O   . HOH J .   ? 0.3536 0.2041 0.2208 0.0396  -0.0276 -0.0575 665 HOH A O   
4743 O  O   . HOH J .   ? 0.7843 0.3717 0.3680 -0.1750 -0.0960 0.0618  666 HOH A O   
4744 O  O   . HOH J .   ? 0.3507 0.8643 0.4005 -0.1158 0.0656  0.0179  667 HOH A O   
4745 O  O   . HOH J .   ? 0.3994 0.4529 0.6073 0.0356  -0.0100 -0.1912 668 HOH A O   
4746 O  O   . HOH J .   ? 0.3218 0.7547 0.3948 0.1456  -0.0409 -0.3486 669 HOH A O   
4747 O  O   . HOH J .   ? 0.4070 0.4140 0.3949 -0.0674 0.0214  0.0244  670 HOH A O   
4748 O  O   . HOH J .   ? 0.6835 0.4316 0.5153 0.0897  -0.0863 -0.2350 671 HOH A O   
4749 O  O   . HOH J .   ? 0.3046 0.3890 0.6582 -0.0207 -0.0623 -0.0849 672 HOH A O   
4750 O  O   . HOH J .   ? 0.1463 0.3231 0.3674 -0.1462 -0.1187 -0.0826 673 HOH A O   
4751 O  O   . HOH J .   ? 0.2872 0.5501 0.6496 -0.0498 -0.1045 0.2703  674 HOH A O   
4752 O  O   . HOH J .   ? 0.5448 0.2151 0.3745 -0.0464 -0.1857 0.0401  675 HOH A O   
4753 O  O   . HOH J .   ? 0.6066 0.3685 0.7622 -0.0562 -0.4572 -0.1659 676 HOH A O   
4754 O  O   . HOH J .   ? 0.7207 0.6441 0.5304 -0.2069 0.0451  -0.0858 677 HOH A O   
4755 O  O   . HOH J .   ? 0.6614 0.2851 0.3513 0.1092  -0.0497 -0.1010 678 HOH A O   
4756 O  O   . HOH J .   ? 0.1991 0.3148 0.4950 -0.0453 0.1123  0.0265  679 HOH A O   
4757 O  O   . HOH J .   ? 0.1940 0.2758 0.4522 0.0133  0.1555  -0.0734 680 HOH A O   
4758 O  O   . HOH J .   ? 0.3225 0.3510 0.3849 0.1185  0.0948  0.0132  681 HOH A O   
4759 O  O   . HOH J .   ? 0.1263 0.4992 0.6144 -0.0242 -0.0469 0.0002  682 HOH A O   
4760 O  O   . HOH J .   ? 0.5039 0.4420 0.4314 0.1304  0.0143  0.0974  683 HOH A O   
4761 O  O   . HOH J .   ? 0.2050 0.4389 0.3501 -0.0478 -0.0442 0.0040  684 HOH A O   
4762 O  O   . HOH J .   ? 0.4865 0.6366 0.5601 0.3361  -0.0958 -0.2913 685 HOH A O   
4763 O  O   . HOH J .   ? 0.5891 0.2020 0.5224 -0.0601 0.1008  -0.0025 686 HOH A O   
4764 O  O   . HOH J .   ? 0.2336 0.4886 0.4159 -0.1048 0.0803  -0.1333 687 HOH A O   
4765 O  O   . HOH J .   ? 0.2395 0.1936 0.5375 -0.0562 0.1776  -0.0857 688 HOH A O   
4766 O  O   . HOH J .   ? 0.5743 0.3407 0.3366 -0.1164 -0.0552 -0.0380 689 HOH A O   
4767 O  O   . HOH J .   ? 0.2249 0.3141 0.4424 -0.1298 -0.0394 -0.0535 690 HOH A O   
4768 O  O   . HOH J .   ? 0.2760 0.2757 0.8250 0.0464  -0.0548 -0.2276 691 HOH A O   
4769 O  O   . HOH J .   ? 0.4097 0.5626 0.4872 0.0036  0.2007  0.0553  692 HOH A O   
4770 O  O   . HOH J .   ? 0.3521 0.4859 0.4986 -0.0288 0.0783  -0.2303 693 HOH A O   
4771 O  O   . HOH J .   ? 0.3364 0.5681 0.5255 -0.1902 -0.0958 -0.0983 694 HOH A O   
4772 O  O   . HOH J .   ? 0.5678 0.3712 0.4773 -0.1662 0.2613  -0.2306 695 HOH A O   
4773 O  O   . HOH J .   ? 0.2433 0.4902 0.5626 -0.0405 -0.0983 0.0550  696 HOH A O   
4774 O  O   . HOH J .   ? 0.7363 0.8769 0.5968 -0.1404 -0.2119 -0.0483 697 HOH A O   
4775 O  O   . HOH J .   ? 0.5626 0.6353 0.5968 0.1411  0.2141  -0.0239 698 HOH A O   
4776 O  O   . HOH J .   ? 0.1520 0.4696 0.5906 -0.0851 0.0256  0.0055  699 HOH A O   
4777 O  O   . HOH J .   ? 0.3407 0.4913 0.5405 0.0541  0.0553  0.0322  700 HOH A O   
4778 O  O   . HOH J .   ? 0.4467 0.2517 0.6915 -0.0334 -0.1231 -0.0898 701 HOH A O   
4779 O  O   . HOH J .   ? 0.6559 0.9866 0.7950 -0.2005 0.3480  -0.2232 702 HOH A O   
4780 O  O   . HOH J .   ? 0.6011 0.6522 0.5272 -0.0366 -0.0298 -0.2190 703 HOH A O   
4781 O  O   . HOH K .   ? 0.4408 0.7774 0.6457 0.0749  -0.0297 -0.2675 401 HOH B O   
4782 O  O   . HOH K .   ? 2.0826 6.7724 4.7287 -3.1195 2.2360  -3.7503 402 HOH B O   
4783 O  O   . HOH K .   ? 0.1648 0.4398 0.4536 -0.0544 -0.0655 -0.1618 403 HOH B O   
4784 O  O   . HOH K .   ? 0.3768 0.3156 0.4353 -0.0089 -0.0948 -0.0769 404 HOH B O   
4785 O  O   . HOH K .   ? 0.3908 0.5854 0.4759 -0.0413 0.0570  -0.0500 405 HOH B O   
4786 O  O   . HOH K .   ? 0.2680 0.2619 0.5619 -0.1170 -0.1517 0.0884  406 HOH B O   
4787 O  O   . HOH K .   ? 0.4233 0.7015 0.7450 0.3122  -0.0977 -0.1758 407 HOH B O   
4788 O  O   . HOH K .   ? 0.3143 0.6655 0.3109 0.1606  0.0238  0.0345  408 HOH B O   
4789 O  O   . HOH K .   ? 0.3747 0.3071 0.5850 -0.1268 0.1888  -0.1015 409 HOH B O   
4790 O  O   . HOH K .   ? 0.3479 0.4635 0.5352 0.0565  0.0763  -0.1112 410 HOH B O   
4791 O  O   . HOH K .   ? 0.1901 0.5159 0.6236 -0.0142 0.0800  -0.2136 411 HOH B O   
4792 O  O   . HOH K .   ? 0.1920 0.3102 0.2720 -0.0999 0.0677  -0.0118 412 HOH B O   
4793 O  O   . HOH K .   ? 0.3063 0.2570 0.3582 -0.1016 -0.0084 -0.0525 413 HOH B O   
4794 O  O   . HOH K .   ? 0.1653 0.4852 0.4654 0.0530  0.0696  -0.1724 414 HOH B O   
4795 O  O   . HOH K .   ? 0.2164 0.3074 0.4038 -0.0819 0.0596  0.0624  415 HOH B O   
4796 O  O   . HOH K .   ? 0.6795 0.2929 0.2374 -0.1682 0.0233  -0.0302 416 HOH B O   
4797 O  O   . HOH K .   ? 0.2639 0.5029 0.2892 -0.0218 0.0440  -0.2388 417 HOH B O   
4798 O  O   . HOH K .   ? 0.5108 0.3764 0.4106 -0.0391 0.0255  0.0694  418 HOH B O   
4799 O  O   . HOH K .   ? 0.6036 0.3026 0.7784 0.0498  -0.1188 -0.0106 419 HOH B O   
4800 O  O   . HOH K .   ? 0.7100 0.2644 0.3462 -0.1486 -0.0441 -0.0623 420 HOH B O   
4801 O  O   . HOH K .   ? 0.1226 0.5991 0.2861 -0.0841 0.0353  -0.1696 421 HOH B O   
4802 O  O   . HOH K .   ? 0.1819 0.3598 0.4523 -0.1300 0.0465  -0.0104 422 HOH B O   
4803 O  O   . HOH K .   ? 0.1287 0.3678 0.3970 0.0141  -0.0057 0.0754  423 HOH B O   
4804 O  O   . HOH K .   ? 0.6450 0.5387 0.2943 -0.2864 0.0659  0.0175  424 HOH B O   
4805 O  O   . HOH K .   ? 0.0229 0.1205 0.1532 -0.0432 0.0191  -0.0616 425 HOH B O   
4806 O  O   . HOH K .   ? 0.2882 0.4392 0.4690 -0.1412 0.1747  -0.2591 426 HOH B O   
4807 O  O   . HOH K .   ? 0.2033 0.2960 0.2350 -0.1288 0.0658  -0.0675 427 HOH B O   
4808 O  O   . HOH K .   ? 0.6365 0.6279 0.6172 -0.4168 -0.0326 -0.3604 428 HOH B O   
4809 O  O   . HOH K .   ? 0.7661 0.5641 0.4802 0.2798  -0.2486 -0.1489 429 HOH B O   
4810 O  O   . HOH K .   ? 0.1570 0.6868 0.4672 -0.1694 -0.0309 0.0292  430 HOH B O   
4811 O  O   . HOH K .   ? 0.3159 0.4611 0.4997 -0.1101 0.0751  -0.2100 431 HOH B O   
4812 O  O   . HOH K .   ? 0.2154 0.2938 0.4342 -0.0085 -0.0145 -0.0216 432 HOH B O   
4813 O  O   . HOH K .   ? 0.2891 0.3406 0.3620 -0.0700 0.0397  0.0873  433 HOH B O   
4814 O  O   . HOH K .   ? 0.2096 0.2584 0.2503 -0.1512 -0.0006 -0.0624 434 HOH B O   
4815 O  O   . HOH K .   ? 0.1832 0.3084 0.3055 -0.1118 0.0889  -0.0966 435 HOH B O   
4816 O  O   . HOH K .   ? 0.3739 0.2615 0.5204 -0.0084 -0.0809 -0.0860 436 HOH B O   
4817 O  O   . HOH K .   ? 0.1786 0.1847 0.2904 -0.0179 -0.1191 -0.0712 437 HOH B O   
4818 O  O   . HOH K .   ? 0.4177 0.4748 0.5112 0.1952  -0.0061 -0.1038 438 HOH B O   
4819 O  O   . HOH K .   ? 0.2741 0.2693 0.6541 -0.0989 0.0584  0.0436  439 HOH B O   
4820 O  O   . HOH K .   ? 1.5017 1.6722 0.4800 -0.8029 0.5916  -0.2064 440 HOH B O   
4821 O  O   . HOH K .   ? 0.7785 0.5516 0.6993 0.1233  -0.1083 0.0886  441 HOH B O   
4822 O  O   . HOH K .   ? 0.3263 0.4362 0.3635 -0.2603 -0.0432 -0.0102 442 HOH B O   
4823 O  O   . HOH K .   ? 0.7318 0.2357 0.2937 -0.0854 -0.1465 0.0514  443 HOH B O   
4824 O  O   . HOH K .   ? 0.9266 0.5655 0.2193 -0.2120 0.2096  0.0746  444 HOH B O   
4825 O  O   . HOH K .   ? 0.1019 0.3597 0.4663 -0.0350 0.0212  -0.0119 445 HOH B O   
4826 O  O   . HOH K .   ? 0.2126 0.2343 0.3215 0.0496  -0.0834 -0.1289 446 HOH B O   
4827 O  O   . HOH K .   ? 0.0951 0.2618 0.2429 -0.0600 0.0713  -0.0937 447 HOH B O   
4828 O  O   . HOH K .   ? 0.2369 0.3666 0.2881 0.0974  -0.1111 -0.0782 448 HOH B O   
4829 O  O   . HOH K .   ? 0.2037 0.1940 0.3444 -0.0117 -0.1151 -0.1209 449 HOH B O   
4830 O  O   . HOH K .   ? 0.2076 0.2701 0.3646 -0.0976 0.0933  -0.1497 450 HOH B O   
4831 O  O   . HOH K .   ? 0.1249 0.1340 0.2330 -0.0558 0.0061  -0.0355 451 HOH B O   
4832 O  O   . HOH K .   ? 0.5424 0.3156 0.2649 -0.0383 0.0085  -0.1376 452 HOH B O   
4833 O  O   . HOH K .   ? 0.0383 0.1321 0.1682 -0.0530 -0.0038 -0.0615 453 HOH B O   
4834 O  O   . HOH K .   ? 0.1369 0.3021 0.4306 0.0008  0.0106  -0.0326 454 HOH B O   
4835 O  O   . HOH K .   ? 0.5104 0.2349 0.4260 -0.2191 0.0811  -0.1795 455 HOH B O   
4836 O  O   . HOH K .   ? 0.3061 0.5682 0.6674 -0.1672 -0.0861 0.0582  456 HOH B O   
4837 O  O   . HOH K .   ? 0.1358 0.2645 0.3357 -0.0344 0.1070  -0.0665 457 HOH B O   
4838 O  O   . HOH K .   ? 0.1498 0.2105 0.2800 -0.0523 -0.0602 -0.1508 458 HOH B O   
4839 O  O   . HOH K .   ? 0.1055 0.1730 0.4603 -0.0410 0.0653  -0.0756 459 HOH B O   
4840 O  O   . HOH K .   ? 0.0773 0.2981 0.3583 -0.0098 0.0471  0.0636  460 HOH B O   
4841 O  O   . HOH K .   ? 0.1799 0.2296 0.3201 0.0027  -0.0490 -0.1010 461 HOH B O   
4842 O  O   . HOH K .   ? 0.7300 0.2285 0.2634 -0.1127 -0.0697 -0.0700 462 HOH B O   
4843 O  O   . HOH K .   ? 0.6003 0.4703 0.3361 -0.1941 0.1799  -0.0954 463 HOH B O   
4844 O  O   . HOH K .   ? 0.1430 0.2708 0.4577 -0.0752 -0.0450 -0.0628 464 HOH B O   
4845 O  O   . HOH K .   ? 0.2602 0.3104 0.4449 -0.0681 -0.0400 -0.2024 465 HOH B O   
4846 O  O   . HOH K .   ? 0.3555 0.2069 0.2142 -0.0958 0.0070  -0.0032 466 HOH B O   
4847 O  O   . HOH K .   ? 0.3304 0.3282 0.2100 -0.0491 -0.0798 -0.0590 467 HOH B O   
4848 O  O   . HOH K .   ? 0.2430 0.7210 0.3556 -0.0203 -0.0467 0.1606  468 HOH B O   
4849 O  O   . HOH K .   ? 0.0236 0.1161 0.1375 -0.0397 0.0032  -0.0524 469 HOH B O   
4850 O  O   . HOH K .   ? 0.4047 0.3220 0.4541 0.1106  -0.1076 -0.0789 470 HOH B O   
4851 O  O   . HOH K .   ? 0.3055 0.3360 0.2907 -0.0790 -0.0487 0.0100  471 HOH B O   
4852 O  O   . HOH K .   ? 0.6312 0.4654 0.4066 -0.1362 0.0952  -0.0717 472 HOH B O   
4853 O  O   . HOH K .   ? 0.2861 0.2693 0.2920 -0.0941 0.0800  -0.0472 473 HOH B O   
4854 O  O   . HOH K .   ? 0.0396 0.1369 0.1614 -0.0609 0.0177  -0.0599 474 HOH B O   
4855 O  O   . HOH K .   ? 0.3247 0.2091 0.3510 -0.1142 0.0697  -0.0562 475 HOH B O   
4856 O  O   . HOH K .   ? 0.1755 0.6573 0.4888 -0.0554 -0.1221 -0.0923 476 HOH B O   
4857 O  O   . HOH K .   ? 0.3538 0.4225 0.6278 -0.1351 -0.0122 -0.2245 477 HOH B O   
4858 O  O   . HOH K .   ? 0.2409 0.2722 0.3948 -0.1244 0.0804  -0.1005 478 HOH B O   
4859 O  O   . HOH K .   ? 0.5044 0.4898 0.7210 0.0281  0.0082  0.1225  479 HOH B O   
4860 O  O   . HOH K .   ? 0.2142 0.2843 0.3948 -0.0085 -0.0033 -0.0704 480 HOH B O   
4861 O  O   . HOH K .   ? 0.1247 0.3432 0.6268 -0.0959 -0.0531 -0.0701 481 HOH B O   
4862 O  O   . HOH K .   ? 0.0263 0.1801 0.1846 -0.0504 -0.0127 -0.0259 482 HOH B O   
4863 O  O   . HOH K .   ? 0.1879 0.3967 0.3089 -0.1289 0.0127  -0.0027 483 HOH B O   
4864 O  O   . HOH K .   ? 0.0221 0.1391 0.1689 -0.0453 0.0249  -0.0545 484 HOH B O   
4865 O  O   . HOH K .   ? 0.1394 0.4768 0.6310 -0.0337 -0.0008 0.0924  485 HOH B O   
4866 O  O   . HOH K .   ? 0.2988 0.2139 0.3418 0.0582  -0.0983 -0.0675 486 HOH B O   
4867 O  O   . HOH K .   ? 0.0217 0.2166 0.3692 -0.0534 0.0067  -0.1163 487 HOH B O   
4868 O  O   . HOH K .   ? 0.1273 0.4066 0.3745 -0.0927 0.0845  -0.0291 488 HOH B O   
4869 O  O   . HOH K .   ? 0.2176 0.1454 0.2316 -0.0910 0.0019  -0.0582 489 HOH B O   
4870 O  O   . HOH K .   ? 0.0158 0.1295 0.1619 -0.0322 0.0063  -0.0665 490 HOH B O   
4871 O  O   . HOH K .   ? 0.1483 0.2073 0.3711 -0.0475 0.0337  -0.0702 491 HOH B O   
4872 O  O   . HOH K .   ? 0.2920 0.2991 0.7497 0.0140  -0.1713 -0.0205 492 HOH B O   
4873 O  O   . HOH K .   ? 0.3357 0.4854 0.8560 0.1048  -0.0589 -0.1067 493 HOH B O   
4874 O  O   . HOH K .   ? 0.3137 0.5209 0.3587 0.0164  0.0688  0.0861  494 HOH B O   
4875 O  O   . HOH K .   ? 0.3970 0.2468 0.2837 -0.0569 -0.1885 -0.0243 495 HOH B O   
4876 O  O   . HOH K .   ? 0.1276 0.2033 0.2266 -0.0553 0.0103  -0.0839 496 HOH B O   
4877 O  O   . HOH K .   ? 0.0669 0.1750 0.2167 -0.0298 0.0139  -0.0270 497 HOH B O   
4878 O  O   . HOH K .   ? 0.1427 0.3432 0.2066 -0.0139 0.0209  -0.0611 498 HOH B O   
4879 O  O   . HOH K .   ? 0.7149 0.2018 0.2275 -0.0837 0.0025  -0.0270 499 HOH B O   
4880 O  O   . HOH K .   ? 0.2072 0.1905 0.8034 -0.0480 -0.1390 0.1086  500 HOH B O   
4881 O  O   . HOH K .   ? 0.4968 0.3024 0.5258 -0.0780 0.0611  0.0345  501 HOH B O   
4882 O  O   . HOH K .   ? 0.0247 0.2241 0.3884 -0.0525 0.0184  -0.0543 502 HOH B O   
4883 O  O   . HOH K .   ? 0.5175 0.3625 0.5502 -0.2154 0.1814  -0.0927 503 HOH B O   
4884 O  O   . HOH K .   ? 0.2967 0.3741 0.3037 -0.1347 -0.1223 0.0370  504 HOH B O   
4885 O  O   . HOH K .   ? 0.0732 0.1906 0.4183 -0.0964 -0.0625 -0.0359 505 HOH B O   
4886 O  O   . HOH K .   ? 0.3362 0.4028 0.5443 -0.0773 -0.1719 0.0051  506 HOH B O   
4887 O  O   . HOH K .   ? 0.1782 0.2393 0.3917 -0.0695 -0.0330 -0.0571 507 HOH B O   
4888 O  O   . HOH K .   ? 0.2364 0.2996 0.2797 -0.1128 -0.0647 -0.0434 508 HOH B O   
4889 O  O   . HOH K .   ? 0.6395 0.6802 0.8549 0.2821  -0.0791 -0.1375 509 HOH B O   
4890 O  O   . HOH K .   ? 0.3034 0.2387 0.3148 -0.1324 -0.0597 -0.0148 510 HOH B O   
4891 O  O   . HOH K .   ? 0.0628 0.2055 0.2272 -0.0237 0.0154  -0.0431 511 HOH B O   
4892 O  O   . HOH K .   ? 0.1238 0.3606 0.3461 -0.1070 0.1128  -0.1544 512 HOH B O   
4893 O  O   . HOH K .   ? 0.4268 0.9371 0.3197 -0.1382 0.0507  -0.1098 513 HOH B O   
4894 O  O   . HOH K .   ? 0.1619 0.2083 0.1868 -0.0261 0.0088  -0.0587 514 HOH B O   
4895 O  O   . HOH K .   ? 0.1456 0.4168 0.3987 -0.1003 -0.0854 -0.0154 515 HOH B O   
4896 O  O   . HOH K .   ? 0.1813 0.1870 0.4759 -0.0079 -0.0236 -0.1747 516 HOH B O   
4897 O  O   . HOH K .   ? 0.1568 0.6520 0.5168 0.1095  -0.0580 -0.2359 517 HOH B O   
4898 O  O   . HOH K .   ? 0.6806 0.5489 0.5389 0.0895  0.1703  0.0861  518 HOH B O   
4899 O  O   . HOH K .   ? 0.3351 0.5931 0.3836 -0.1236 0.0278  0.1701  519 HOH B O   
4900 O  O   . HOH K .   ? 0.4454 0.6370 0.6566 -0.2165 0.0851  -0.0412 520 HOH B O   
4901 O  O   . HOH K .   ? 0.1466 0.3057 0.3923 -0.0529 -0.0649 -0.0553 521 HOH B O   
4902 O  O   . HOH K .   ? 0.4969 0.5698 0.6383 -0.1731 -0.0353 -0.0788 522 HOH B O   
4903 O  O   . HOH K .   ? 0.3163 0.2753 0.3190 -0.1270 0.0992  -0.0055 523 HOH B O   
4904 O  O   . HOH K .   ? 0.0321 0.1545 0.1852 -0.0249 0.0049  -0.0435 524 HOH B O   
4905 O  O   . HOH K .   ? 0.2156 0.2449 0.2814 0.0670  -0.0712 -0.0763 525 HOH B O   
4906 O  O   . HOH K .   ? 0.1342 0.2943 0.2947 -0.0743 -0.0355 -0.0328 526 HOH B O   
4907 O  O   . HOH K .   ? 0.2007 0.3110 0.4206 -0.0651 0.0930  0.0402  527 HOH B O   
4908 O  O   . HOH K .   ? 0.1676 0.5422 0.4914 -0.0772 -0.0734 -0.0013 528 HOH B O   
4909 O  O   . HOH K .   ? 0.3049 0.4333 0.6406 -0.0151 -0.0696 -0.0051 529 HOH B O   
4910 O  O   . HOH K .   ? 0.2176 0.2434 0.5632 0.0034  -0.0547 -0.0313 530 HOH B O   
4911 O  O   . HOH K .   ? 0.2582 0.6583 0.2938 0.1207  0.0690  0.1395  531 HOH B O   
4912 O  O   . HOH K .   ? 0.1980 0.4285 0.6120 -0.0156 0.1662  -0.0556 532 HOH B O   
4913 O  O   . HOH K .   ? 0.4900 0.3604 0.2577 -0.1437 0.1116  -0.0734 533 HOH B O   
4914 O  O   . HOH K .   ? 0.3107 0.8854 0.3705 -0.0013 0.0853  0.1020  534 HOH B O   
4915 O  O   . HOH K .   ? 0.0139 0.2587 0.3309 -0.0401 0.0039  -0.1329 535 HOH B O   
4916 O  O   . HOH K .   ? 0.0867 0.5011 0.6881 -0.0031 0.0182  -0.0471 536 HOH B O   
4917 O  O   . HOH K .   ? 0.2163 0.4060 0.3115 0.0891  0.0925  0.0029  537 HOH B O   
4918 O  O   . HOH K .   ? 0.2976 0.3183 0.9189 0.0434  -0.0498 -0.2929 538 HOH B O   
4919 O  O   . HOH K .   ? 0.0666 0.2063 0.2998 -0.0715 0.0820  -0.0680 539 HOH B O   
4920 O  O   . HOH K .   ? 0.2773 0.2585 0.3567 -0.0421 0.1771  -0.0890 540 HOH B O   
4921 O  O   . HOH K .   ? 0.0543 0.2302 0.3031 -0.0987 0.0079  -0.0944 541 HOH B O   
4922 O  O   . HOH K .   ? 0.1265 0.1915 0.2549 -0.0375 -0.0282 -0.0993 542 HOH B O   
4923 O  O   . HOH K .   ? 0.3034 0.2642 0.2796 -0.1192 0.1323  -0.0811 543 HOH B O   
4924 O  O   . HOH K .   ? 0.0503 0.3714 0.3908 -0.0536 0.0554  -0.0684 544 HOH B O   
4925 O  O   . HOH K .   ? 0.1971 0.4346 0.3718 0.1116  0.0943  0.0115  545 HOH B O   
4926 O  O   . HOH K .   ? 0.3647 0.2365 0.3203 0.0299  0.0708  -0.0219 546 HOH B O   
4927 O  O   . HOH K .   ? 0.3888 0.3466 0.2567 0.1939  -0.0324 -0.0253 547 HOH B O   
4928 O  O   . HOH K .   ? 0.8595 0.4782 0.4213 -0.2408 0.1980  -0.0570 548 HOH B O   
4929 O  O   . HOH K .   ? 0.2893 0.3325 0.3172 -0.1179 0.1514  -0.1540 549 HOH B O   
4930 O  O   . HOH K .   ? 0.5164 0.2706 0.2615 -0.0900 -0.1884 -0.0521 550 HOH B O   
4931 O  O   . HOH K .   ? 0.1331 0.2877 0.3149 -0.0420 -0.0024 0.0150  551 HOH B O   
4932 O  O   . HOH K .   ? 0.4527 0.3773 0.5981 -0.1365 0.2029  -0.2316 552 HOH B O   
4933 O  O   . HOH K .   ? 0.1797 0.3161 0.7155 0.0241  0.0954  -0.0491 553 HOH B O   
4934 O  O   . HOH K .   ? 0.5371 0.2885 0.3964 -0.0342 -0.0592 -0.0835 554 HOH B O   
4935 O  O   . HOH K .   ? 0.2766 0.2100 0.2610 -0.0473 -0.1196 -0.0054 555 HOH B O   
4936 O  O   . HOH K .   ? 0.6308 0.3079 0.4277 -0.0075 -0.0078 -0.1247 556 HOH B O   
4937 O  O   . HOH K .   ? 0.5498 0.3746 0.3984 -0.2168 0.0047  -0.1776 557 HOH B O   
4938 O  O   . HOH K .   ? 0.2169 0.5006 0.4806 0.0946  -0.0245 -0.0787 558 HOH B O   
4939 O  O   . HOH K .   ? 0.4783 0.1527 0.2644 -0.1004 -0.1116 -0.0296 559 HOH B O   
4940 O  O   . HOH K .   ? 0.2565 0.4235 0.5856 0.0239  0.0084  -0.0634 560 HOH B O   
4941 O  O   . HOH K .   ? 0.1068 0.3878 0.3925 0.0345  -0.0359 -0.1026 561 HOH B O   
4942 O  O   . HOH K .   ? 0.0200 0.2461 0.2433 -0.0321 -0.0433 -0.0272 562 HOH B O   
4943 O  O   . HOH K .   ? 0.2218 0.1538 0.2523 -0.0745 -0.0606 -0.0985 563 HOH B O   
4944 O  O   . HOH K .   ? 0.1012 0.2840 0.3847 -0.0907 0.0731  -0.1099 564 HOH B O   
4945 O  O   . HOH K .   ? 0.2332 0.6009 0.5889 -0.1245 -0.0803 -0.0342 565 HOH B O   
4946 O  O   . HOH K .   ? 0.2226 0.4755 0.4953 -0.1235 0.0583  0.0226  566 HOH B O   
4947 O  O   . HOH K .   ? 0.3371 0.2477 0.2277 0.0794  0.0250  -0.0378 567 HOH B O   
4948 O  O   . HOH K .   ? 0.2512 0.6205 0.6685 -0.0375 -0.0205 -0.0167 568 HOH B O   
4949 O  O   . HOH K .   ? 0.6706 0.7572 0.6348 0.2383  0.4347  0.1912  569 HOH B O   
4950 O  O   . HOH K .   ? 0.1667 0.3731 0.5357 0.0098  -0.0039 -0.0177 570 HOH B O   
4951 O  O   . HOH K .   ? 0.0488 0.2745 0.4031 -0.0057 -0.0092 -0.0023 571 HOH B O   
4952 O  O   . HOH K .   ? 0.2361 0.2266 0.3221 -0.0201 0.0983  0.0312  572 HOH B O   
4953 O  O   . HOH K .   ? 0.3714 0.3775 0.3718 0.0749  -0.1538 -0.1668 573 HOH B O   
4954 O  O   . HOH K .   ? 0.2751 0.3913 0.5954 -0.0668 -0.1381 -0.0317 574 HOH B O   
4955 O  O   . HOH K .   ? 0.4768 0.3854 0.4339 -0.0450 -0.0182 -0.0766 575 HOH B O   
4956 O  O   . HOH K .   ? 0.2913 0.3788 0.8097 -0.0211 0.0228  -0.2663 576 HOH B O   
4957 O  O   . HOH K .   ? 0.0248 0.1416 0.1724 -0.0380 0.0043  -0.0560 577 HOH B O   
4958 O  O   . HOH K .   ? 0.4636 0.1984 0.3156 -0.0992 -0.1483 0.0004  578 HOH B O   
4959 O  O   . HOH K .   ? 0.4580 0.3310 0.3838 0.1271  0.0836  -0.0705 579 HOH B O   
4960 O  O   . HOH K .   ? 0.7370 0.4634 0.2833 0.2096  -0.1073 -0.0534 580 HOH B O   
4961 O  O   . HOH K .   ? 0.3614 0.1841 0.3134 0.0380  0.0947  -0.0190 581 HOH B O   
4962 O  O   . HOH K .   ? 0.1901 0.1876 0.2840 -0.0097 0.0293  -0.0738 582 HOH B O   
4963 O  O   . HOH K .   ? 0.2022 0.2742 0.3203 0.0253  0.0601  -0.0125 583 HOH B O   
4964 O  O   . HOH K .   ? 0.2106 0.3572 0.4498 -0.0245 -0.0311 -0.0841 584 HOH B O   
4965 O  O   . HOH K .   ? 0.4727 0.2549 0.7578 -0.0301 0.2126  -0.1733 585 HOH B O   
4966 O  O   . HOH K .   ? 0.3687 0.2135 0.7342 -0.0534 0.1129  -0.0326 586 HOH B O   
4967 O  O   . HOH K .   ? 0.5636 0.6315 0.4257 0.3175  -0.0095 -0.1693 587 HOH B O   
4968 O  O   . HOH K .   ? 0.0351 0.2238 0.3388 -0.0485 -0.0198 -0.0673 588 HOH B O   
4969 O  O   . HOH K .   ? 0.1415 0.3188 0.5371 0.0253  0.0332  -0.0233 589 HOH B O   
4970 O  O   . HOH K .   ? 0.1936 0.3617 0.4995 -0.1511 0.1092  0.0034  590 HOH B O   
4971 O  O   . HOH K .   ? 0.4268 0.4259 0.5928 -0.1737 -0.0084 0.0359  591 HOH B O   
4972 O  O   . HOH K .   ? 0.2279 0.2014 0.6596 0.0168  0.0611  -0.1858 592 HOH B O   
4973 O  O   . HOH K .   ? 0.2441 0.4418 0.4008 -0.1747 0.0330  -0.0251 593 HOH B O   
4974 O  O   . HOH K .   ? 0.2332 0.5585 0.4394 0.0145  -0.1177 -0.3246 594 HOH B O   
4975 O  O   . HOH K .   ? 0.4269 0.3486 0.2518 -0.0111 -0.1048 -0.1125 595 HOH B O   
4976 O  O   . HOH K .   ? 0.3209 0.5103 0.4888 -0.0150 -0.0363 -0.2008 596 HOH B O   
4977 O  O   . HOH K .   ? 0.7135 0.6718 0.6342 0.0071  0.0850  -0.0610 597 HOH B O   
4978 O  O   . HOH K .   ? 0.3889 0.4130 0.4246 -0.0861 0.1573  0.0314  598 HOH B O   
4979 O  O   . HOH K .   ? 0.3643 0.6564 0.3749 -0.2281 0.0601  -0.0250 599 HOH B O   
4980 O  O   . HOH K .   ? 0.5309 0.1838 0.2782 -0.0712 -0.1693 -0.0023 600 HOH B O   
4981 O  O   . HOH K .   ? 0.3364 0.6047 0.6065 0.0243  0.0841  0.1310  601 HOH B O   
4982 O  O   . HOH K .   ? 0.7445 0.3962 0.2345 -0.0322 0.1626  -0.0379 602 HOH B O   
4983 O  O   . HOH K .   ? 0.2129 0.4163 0.3325 0.0882  0.0273  -0.0075 603 HOH B O   
4984 O  O   . HOH K .   ? 0.3578 0.3511 0.2696 -0.0054 -0.0628 -0.0995 604 HOH B O   
4985 O  O   . HOH K .   ? 0.0964 0.1627 0.2591 -0.0547 -0.0405 -0.0532 605 HOH B O   
4986 O  O   . HOH K .   ? 0.3551 0.6934 0.5342 0.0053  0.0621  -0.3925 606 HOH B O   
4987 O  O   . HOH K .   ? 0.4051 0.6488 0.3802 -0.2118 -0.0517 -0.0284 607 HOH B O   
4988 O  O   . HOH K .   ? 0.7044 0.7980 0.3445 0.2709  0.0249  -0.0452 608 HOH B O   
4989 O  O   . HOH K .   ? 0.2991 0.4788 0.6973 0.0227  -0.0614 -0.3274 609 HOH B O   
4990 O  O   . HOH K .   ? 0.1847 0.4934 0.4220 -0.1451 0.0886  -0.1340 610 HOH B O   
4991 O  O   . HOH K .   ? 0.4354 0.4759 0.4772 -0.0454 0.1455  0.0179  611 HOH B O   
4992 O  O   . HOH K .   ? 0.4889 0.4220 0.3840 0.0955  0.0022  -0.0836 612 HOH B O   
4993 O  O   . HOH K .   ? 0.3288 0.4349 0.4560 0.0406  0.1767  -0.0695 613 HOH B O   
4994 O  O   . HOH K .   ? 0.7242 0.3468 0.4086 0.0961  0.1830  0.0070  614 HOH B O   
4995 O  O   . HOH K .   ? 0.2419 0.3297 0.6769 -0.0350 -0.1072 0.0620  615 HOH B O   
4996 O  O   . HOH K .   ? 0.2113 0.2442 0.5511 -0.0609 0.1295  -0.1102 616 HOH B O   
4997 O  O   . HOH K .   ? 0.2996 0.6010 0.5741 -0.1300 0.0239  0.0652  617 HOH B O   
4998 O  O   . HOH K .   ? 0.3731 0.2725 0.5895 0.0305  0.2250  0.0588  618 HOH B O   
4999 O  O   . HOH K .   ? 0.9304 0.4028 0.2643 -0.1800 0.0198  -0.0466 619 HOH B O   
5000 O  O   . HOH K .   ? 0.2224 0.3917 0.4234 0.0403  0.0381  0.0868  620 HOH B O   
5001 O  O   . HOH K .   ? 0.2615 0.8052 0.5987 -0.1531 0.0613  -0.1982 621 HOH B O   
5002 O  O   . HOH K .   ? 0.1771 0.3713 0.4046 -0.0412 0.0301  -0.0104 622 HOH B O   
5003 O  O   . HOH K .   ? 0.4631 0.6403 0.7888 0.1234  -0.0314 -0.0326 623 HOH B O   
5004 O  O   . HOH K .   ? 0.3278 0.7764 0.3127 -0.0832 0.0674  -0.1830 624 HOH B O   
5005 O  O   . HOH K .   ? 0.2672 0.6945 0.4038 -0.1187 -0.0638 0.2017  625 HOH B O   
5006 O  O   . HOH K .   ? 0.1326 0.3003 0.4498 -0.1097 0.0131  -0.0788 626 HOH B O   
5007 O  O   . HOH K .   ? 0.3395 0.2066 0.2240 -0.1359 -0.0190 -0.0217 627 HOH B O   
5008 O  O   . HOH K .   ? 0.2421 0.2947 0.4849 0.0810  -0.2186 -0.1376 628 HOH B O   
5009 O  O   . HOH K .   ? 0.4825 0.4940 0.6009 0.2145  -0.0370 -0.1061 629 HOH B O   
5010 O  O   . HOH K .   ? 0.5814 0.9288 0.5327 -0.2049 -0.0084 -0.0754 630 HOH B O   
5011 O  O   . HOH K .   ? 0.3279 0.3984 0.5327 -0.2486 0.0279  0.0143  631 HOH B O   
5012 O  O   . HOH K .   ? 0.5625 0.5485 0.4393 0.1042  0.2136  0.0340  632 HOH B O   
5013 O  O   . HOH K .   ? 0.4099 0.5881 0.7113 -0.1487 -0.1603 0.1072  633 HOH B O   
5014 O  O   . HOH K .   ? 0.7727 0.2772 0.2990 0.0993  0.0539  -0.0286 634 HOH B O   
5015 O  O   . HOH K .   ? 0.5444 0.5297 0.2954 0.0495  0.0411  0.0200  635 HOH B O   
5016 O  O   . HOH K .   ? 0.2504 0.3285 0.4917 -0.1200 0.0405  -0.0389 636 HOH B O   
5017 O  O   . HOH K .   ? 0.3404 0.5234 0.6659 0.1393  0.1145  0.0340  637 HOH B O   
5018 O  O   . HOH K .   ? 0.2308 0.5884 0.5129 -0.1499 0.0273  0.0433  638 HOH B O   
5019 O  O   . HOH K .   ? 0.1659 0.3171 0.2663 -0.1366 -0.0231 -0.0591 639 HOH B O   
5020 O  O   . HOH K .   ? 0.0825 0.3119 0.4228 0.0115  0.0853  -0.0297 640 HOH B O   
5021 O  O   . HOH K .   ? 0.4012 0.3920 0.3094 0.0351  -0.0091 -0.1725 641 HOH B O   
5022 O  O   . HOH K .   ? 0.4541 0.3980 0.4503 0.0381  0.0400  0.0729  642 HOH B O   
5023 O  O   . HOH K .   ? 0.3261 0.4820 0.4862 -0.1944 -0.1964 0.0350  643 HOH B O   
5024 O  O   . HOH K .   ? 0.2698 0.6186 0.3723 0.1266  -0.0917 -0.0683 644 HOH B O   
5025 O  O   . HOH K .   ? 0.2192 0.2866 0.4018 -0.1404 -0.0258 -0.0421 645 HOH B O   
5026 O  O   . HOH K .   ? 0.0954 0.3858 0.6983 -0.0149 -0.0618 -0.0508 646 HOH B O   
5027 O  O   . HOH K .   ? 0.1978 0.5861 0.5179 -0.0509 -0.0627 -0.2449 647 HOH B O   
5028 O  O   . HOH K .   ? 0.3235 0.4288 0.5206 -0.0881 -0.0012 -0.1043 648 HOH B O   
5029 O  O   . HOH K .   ? 0.2110 0.3274 0.4330 0.0417  -0.0163 -0.1076 649 HOH B O   
5030 O  O   . HOH K .   ? 0.4539 0.5475 0.5612 0.0331  0.0627  0.1375  650 HOH B O   
5031 O  O   . HOH K .   ? 0.1434 0.5453 0.4844 0.0092  -0.0350 -0.0650 651 HOH B O   
5032 O  O   . HOH K .   ? 0.3827 0.2550 0.3898 -0.0209 0.0127  -0.0949 652 HOH B O   
5033 O  O   . HOH K .   ? 0.2337 0.3509 0.6093 -0.0974 0.0871  0.0590  653 HOH B O   
5034 O  O   . HOH K .   ? 0.1544 0.6205 0.3153 0.0925  -0.0157 -0.0504 654 HOH B O   
5035 O  O   . HOH K .   ? 0.3128 0.6082 0.2802 0.0354  0.1027  -0.0257 655 HOH B O   
5036 O  O   . HOH K .   ? 0.6416 0.3072 0.7124 -0.1544 0.0505  0.0551  656 HOH B O   
5037 O  O   . HOH K .   ? 0.1482 0.2563 0.4512 -0.0491 0.0038  -0.0622 657 HOH B O   
5038 O  O   . HOH K .   ? 0.5207 0.2984 0.7846 0.0026  0.0512  -0.0521 658 HOH B O   
5039 O  O   . HOH K .   ? 0.4970 0.3458 0.5092 -0.0550 -0.0384 -0.0296 659 HOH B O   
5040 O  O   . HOH K .   ? 0.2511 0.2938 0.7135 -0.0109 -0.0784 -0.0116 660 HOH B O   
5041 O  O   . HOH K .   ? 0.1482 0.2190 0.2457 -0.0669 0.0027  -0.0173 661 HOH B O   
5042 O  O   . HOH K .   ? 0.9424 0.3443 1.0267 0.1376  -0.2546 -0.1025 662 HOH B O   
5043 O  O   . HOH K .   ? 0.2482 0.2256 0.3840 -0.0373 0.0633  0.0378  663 HOH B O   
5044 O  O   . HOH K .   ? 0.4046 0.4598 0.3558 -0.0316 0.0326  -0.0238 664 HOH B O   
5045 O  O   . HOH K .   ? 0.3484 0.3143 0.6776 -0.0511 -0.1386 -0.0873 665 HOH B O   
5046 O  O   . HOH K .   ? 0.6158 0.4164 0.6567 -0.1401 -0.3010 0.1837  666 HOH B O   
5047 O  O   . HOH K .   ? 0.4219 0.7238 0.4600 -0.2673 0.0956  -0.0895 667 HOH B O   
5048 O  O   . HOH K .   ? 0.4419 0.3559 0.5517 0.0661  -0.1167 -0.2791 668 HOH B O   
5049 O  O   . HOH K .   ? 0.5682 0.4878 0.4647 -0.1194 -0.1202 -0.1399 669 HOH B O   
5050 O  O   . HOH K .   ? 0.2437 0.4347 0.5697 -0.0634 -0.1163 -0.1375 670 HOH B O   
5051 O  O   . HOH K .   ? 0.2197 0.5101 0.5162 -0.0663 0.0527  -0.1360 671 HOH B O   
5052 O  O   . HOH K .   ? 0.3419 0.4301 0.4026 0.1395  0.0893  0.0211  672 HOH B O   
5053 O  O   . HOH K .   ? 0.3648 0.4572 0.4996 0.0546  0.0311  -0.0084 673 HOH B O   
5054 O  O   . HOH K .   ? 0.3206 0.4331 0.4666 -0.0258 -0.0209 -0.0200 674 HOH B O   
5055 O  O   . HOH K .   ? 0.3361 0.3960 0.4279 -0.0911 0.0233  -0.0478 675 HOH B O   
5056 O  O   . HOH K .   ? 0.1046 0.2766 0.2448 0.0250  -0.0507 -0.0377 676 HOH B O   
5057 O  O   . HOH K .   ? 0.2316 0.5802 0.5739 -0.0480 -0.0284 -0.1420 677 HOH B O   
5058 O  O   . HOH K .   ? 0.4528 0.7422 0.5083 -0.0439 -0.0596 0.0278  678 HOH B O   
5059 O  O   . HOH K .   ? 0.6100 0.6473 0.5175 -0.0774 0.0469  0.0222  679 HOH B O   
5060 O  O   . HOH K .   ? 0.2812 0.3459 0.5364 -0.0122 0.0916  0.1288  680 HOH B O   
5061 O  O   . HOH K .   ? 0.4914 0.3397 0.5872 -0.1664 -0.2172 -0.0512 681 HOH B O   
5062 O  O   . HOH K .   ? 0.3269 0.2829 0.9089 -0.1054 -0.0908 -0.0389 682 HOH B O   
5063 O  O   . HOH K .   ? 0.1490 0.6373 0.5894 0.0092  0.0414  0.0259  683 HOH B O   
5064 O  O   . HOH K .   ? 0.4989 0.2645 0.4465 0.0194  -0.1573 -0.1020 684 HOH B O   
5065 O  O   . HOH K .   ? 0.1908 0.3393 0.3829 -0.1085 0.1285  -0.0391 685 HOH B O   
5066 O  O   . HOH K .   ? 0.2843 0.4455 0.6718 -0.0311 0.1060  0.0118  686 HOH B O   
5067 O  O   . HOH K .   ? 0.4925 0.2386 0.4196 -0.2039 0.0493  -0.0824 687 HOH B O   
5068 O  O   . HOH K .   ? 0.4233 0.3238 0.6595 -0.1433 -0.0057 0.1218  688 HOH B O   
5069 O  O   . HOH K .   ? 0.1672 0.2339 0.4413 -0.0530 0.0316  -0.0933 689 HOH B O   
5070 O  O   . HOH K .   ? 0.5964 0.3660 0.5317 -0.0058 -0.1452 -0.1034 690 HOH B O   
5071 O  O   . HOH K .   ? 0.3291 0.5422 0.3352 -0.0719 -0.0768 -0.0148 691 HOH B O   
5072 O  O   . HOH K .   ? 0.4721 0.3538 0.4710 0.0533  0.2156  0.1085  692 HOH B O   
5073 O  O   . HOH K .   ? 0.3173 0.4645 0.7734 -0.0825 0.1233  -0.2318 693 HOH B O   
5074 O  O   . HOH K .   ? 0.2676 0.5120 0.6700 -0.0730 -0.1458 -0.1061 694 HOH B O   
5075 O  O   . HOH K .   ? 0.3902 0.5565 0.4697 0.0250  0.0340  0.1111  695 HOH B O   
5076 O  O   . HOH K .   ? 0.1914 0.8538 0.6973 -0.1852 0.0933  0.0106  696 HOH B O   
5077 O  O   . HOH K .   ? 0.3195 0.7576 0.3644 -0.0166 -0.0104 0.0219  697 HOH B O   
5078 O  O   . HOH K .   ? 0.3997 0.4209 0.5133 0.1269  0.0232  -0.1368 698 HOH B O   
5079 O  O   . HOH K .   ? 0.9668 0.3046 0.7005 -0.0518 -0.3470 -0.0046 699 HOH B O   
# 
